NDUFA4 Antibody Cat

Total Page:16

File Type:pdf, Size:1020Kb

NDUFA4 Antibody Cat NDUFA4 Antibody Cat. No.: 16-185 NDUFA4 Antibody Immunofluorescence analysis of L929 cells using NDUFA4 Immunofluorescence analysis of U-2 OS cells using Polyclonal Antibody (16-185) at dilution of 1:100 (40x lens). NDUFA4 Polyclonal Antibody (16-185) at dilution of 1:100 Blue: DAPI for nuclear staining. (40x lens). Blue: DAPI for nuclear staining. Specifications HOST SPECIES: Rabbit SPECIES REACTIVITY: Human, Mouse, Rat Recombinant fusion protein containing a sequence corresponding to amino acids 1-81 of IMMUNOGEN: human NDUFA4 (NP_002480.1). TESTED APPLICATIONS: IF, WB WB: ,1:500 - 1:2000 APPLICATIONS: IF: ,1:50 - 1:100 POSITIVE CONTROL: 1) U-251MG September 27, 2021 1 https://www.prosci-inc.com/ndufa4-antibody-16-185.html 2) HepG2 3) HeLa 4) Mouse intestine 5) Mouse brain 6) Mouse heart PREDICTED MOLECULAR Observed: 12kDa WEIGHT: Properties PURIFICATION: Affinity purification CLONALITY: Polyclonal ISOTYPE: IgG CONJUGATE: Unconjugated PHYSICAL STATE: Liquid BUFFER: PBS with 0.02% sodium azide, 50% glycerol, pH7.3. STORAGE CONDITIONS: Store at -20˚C. Avoid freeze / thaw cycles. Additional Info OFFICIAL SYMBOL: NDUFA4 CI-9k, CI-MLRQ, COXFA4, MLRQ, cytochrome c oxidase subunit NDUFA4, Complex I 9kDa subunit, NADH dehydrogenase (ubiquinone) 1 alpha subcomplex, 4, 9kDa, NADH ALTERNATE NAMES: dehydrogenase [ubiquinone] 1 alpha subcomplex subunit 4, NADH-ubiquinone oxidoreductase MLRQ subunit, complex I-MLRQ, cytochrome c oxidase subunit FA4 GENE ID: 4697 USER NOTE: Optimal dilutions for each application to be determined by the researcher. Background and References The protein encoded by this gene belongs to the complex I 9kDa subunit family. Mammalian complex I of mitochondrial respiratory chain is composed of 45 different BACKGROUND: subunits. This protein has NADH dehydrogenase activity and oxidoreductase activity. It transfers electrons from NADH to the respiratory chain. The immediate electron acceptor for the enzyme is believed to be ubiquinone. ANTIBODIES FOR RESEARCH USE ONLY. September 27, 2021 2 https://www.prosci-inc.com/ndufa4-antibody-16-185.html For additional information, visit ProSci's Terms & Conditions Page. September 27, 2021 3 https://www.prosci-inc.com/ndufa4-antibody-16-185.html.
Recommended publications
  • Proteomic Analysis of the Role of the Quality Control Protease LONP1 in Mitochondrial Protein Aggregation
    bioRxiv preprint doi: https://doi.org/10.1101/2021.04.12.439502; this version posted April 16, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity. It is made available under aCC-BY-NC-ND 4.0 International license. Proteomic analysis of the role of the quality control protease LONP1 in mitochondrial protein aggregation Karen Pollecker1, Marc Sylvester2 and Wolfgang Voos1,* 1Institute of Biochemistry and Molecular Biology (IBMB), University of Bonn, Faculty of Medicine, Nussallee 11, 53115 Bonn, Germany 2Core facility for mass spectrometry, Institute of Biochemistry and Molecular Biology (IBMB), University of Bonn, Faculty of Medicine, Nussallee 11, 53115 Bonn, Germany *Corresponding author Email: [email protected] Phone: +49-228-732426 Abbreviations: AAA+, ATPases associated with a wide variety of cellular activities; Δψ, mitochondrial membrane potential; gKD, genetic knockdown; HSP, heat shock protein; m, mature form; mt, mitochondrial; p, precursor form; PQC, protein quality control; qMS, quantitative mass spectrometry; ROS, reactive oxygen species; SILAC, stable isotope labeling with amino acids in cell culture; siRNA, small interfering RNA; TIM, preprotein translocase complex of the inner membrane; TMRE, tetramethylrhodamine; TOM, preprotein translocase complex of the outer membrane; UPRmt, mitochondrial unfolded protein response; WT, wild type. bioRxiv preprint doi: https://doi.org/10.1101/2021.04.12.439502; this version posted April 16, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder, who has granted bioRxiv a license to display the preprint in perpetuity.
    [Show full text]
  • Structure of the Intact 14-Subunit Human Cytochrome C Oxidase
    www.nature.com/cr www.cell-research.com ARTICLE Structure of the intact 14-subunit human cytochrome c oxidase Shuai Zong 1, Meng Wu1, Jinke Gu1, Tianya Liu1, Runyu Guo1 and Maojun Yang1,2 Respiration is one of the most basic features of living organisms, and the electron transport chain complexes are probably the most complicated protein system in mitochondria. Complex-IV is the terminal enzyme of the electron transport chain, existing either as randomly scattered complexes or as a component of supercomplexes. NDUFA4 was previously assumed as a subunit of complex-I, but recent biochemical data suggested it may be a subunit of complex-IV. However, no structural evidence supporting this notion was available till now. Here we obtained the 3.3 Å resolution structure of complex-IV derived from the human supercomplex I1III2IV1 and assigned the NDUFA4 subunit into complex-IV. Intriguingly, NDUFA4 lies exactly at the dimeric interface observed in previously reported crystal structures of complex-IV homodimer which would preclude complex- IV dimerization. Combining previous structural and biochemical data shown by us and other groups, we propose that the intact complex-IV is a monomer containing 14 subunits. Cell Research (2018) 28:1026–1034; https://doi.org/10.1038/s41422-018-0071-1 INTRODUCTION states under physiological conditions, either being assembled into Mitochondria are critical to many cellular activities. Respiration is supercomplexes or freely scattered on mitochondrial inner the central function of mitochondria, and is exquisitely regulated membrane.36 NDUFA4 was originally considered as a subunit of in multiple ways in response to varying cell conditions.1–3 The Complex-I37 but was proposed to belong to Complex-IV recently.38 assembly of respiratory chain complexes, Complex I–IV (CI, NADH: However, the precise location of NDUFA4 in CIV remains unknown, ubiquinone oxidoreductase; CII, succinate:ubiquinone oxidoreduc- and thus this notion still lacks structural support.
    [Show full text]
  • NDUFA4 Rabbit Pab
    Leader in Biomolecular Solutions for Life Science NDUFA4 Rabbit pAb Catalog No.: A15693 Basic Information Background Catalog No. The protein encoded by this gene belongs to the complex I 9kDa subunit family. A15693 Mammalian complex I of mitochondrial respiratory chain is composed of 45 different subunits. This protein has NADH dehydrogenase activity and oxidoreductase activity. It Observed MW transfers electrons from NADH to the respiratory chain. The immediate electron acceptor 12kDa for the enzyme is believed to be ubiquinone. Calculated MW 9kDa Category Primary antibody Applications WB, IHC, IF Cross-Reactivity Human, Mouse, Rat Recommended Dilutions Immunogen Information WB 1:500 - 1:2000 Gene ID Swiss Prot 4697 O00483 IHC 1:50 - 1:200 Immunogen 1:50 - 1:100 IF Recombinant fusion protein containing a sequence corresponding to amino acids 1-81 of human NDUFA4 (NP_002480.1). Synonyms NDUFA4;CI-9k;CI-MLRQ;MLRQ Contact Product Information www.abclonal.com Source Isotype Purification Rabbit IgG Affinity purification Storage Store at -20℃. Avoid freeze / thaw cycles. Buffer: PBS with 0.02% sodium azide,50% glycerol,pH7.3. Validation Data Western blot analysis of extracts of various cell lines, using NDUFA4 antibody (A15693) at 1:1000 dilution. Secondary antibody: HRP Goat Anti-Rabbit IgG (H+L) (AS014) at 1:10000 dilution. Lysates/proteins: 25ug per lane. Blocking buffer: 3% nonfat dry milk in TBST. Detection: ECL Basic Kit (RM00020). Exposure time: 1s. Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- Immunohistochemistry of paraffin- embedded human liver using NDUFA4 embedded mouse brain using NDUFA4 embedded rat kidney using NDUFA4 Rabbit pAb (A15693) at dilution of 1:100 Rabbit pAb (A15693) at dilution of 1:100 Rabbit pAb (A15693) at dilution of 1:100 (40x lens).
    [Show full text]
  • 1 Alpha Subcomplex 4-Like 2 in Clear Cell Renal Cell Carcinoma Denise R
    Published OnlineFirst January 18, 2016; DOI: 10.1158/1078-0432.CCR-15-1511 Biology of Human Tumors Clinical Cancer Research Role of NADH Dehydrogenase (Ubiquinone) 1 Alpha Subcomplex 4-Like 2 in Clear Cell Renal Cell Carcinoma Denise R. Minton1,2,7, Leiping Fu1, Nigel P. Mongan3, Maria M. Shevchuk4,5, David M. Nanus5,6, and Lorraine J. Gudas1,5 Abstract Purpose: We delineated the functions of the hypoxia-inducible analyzed the proliferation, clonogenicity, metabolite levels, cell factor-1a (HIF1a) target NADH dehydrogenase (ubiquinone) 1 structure, and autophagy in ccRCC cell lines in culture. alpha subcomplex 4-like 2 (NDUFA4L2) in clear cell renal cell Results: We found that NDUFA4L2 mRNA and protein are carcinoma (ccRCC) and characterized NDUFA4L2 as a novel highly expressed in ccRCC samples but undetectable in normal molecular target for ccRCC treatment. kidney tissue samples, and that NDUFA4L2 mRNA expression Experimental Design: We evaluated normal kidney and ccRCC correlates with tumor stage and lower overall survival. In addition, patient microarray and RNAseq data from Oncomine and The we demonstrated that NDUFA4L2 is an HIF1a target in ccRCC Cancer Genome Atlas for NDUFA4L2 mRNA levels and the and that NDUFA4L2 knockdown has a profound antiproliferative clinical implications of high NDUFA4L2 expression. In addition, effect, alters metabolic pathways, and causes major stress in we examined normal kidney and ccRCC patient tissue samples, cultured RCC cells. human ccRCC cell lines, and murine models of ccRCC for NDU- Conclusions: Collectively, our data show that NDUFA4L2 is a FA4L2 mRNA and protein expression. Utilizing short hairpin novel molecular target for ccRCC treatment.
    [Show full text]
  • Reports Report
    Cell Reports Report NDUFA4 Mutations Underlie Dysfunction of a Cytochrome c Oxidase Subunit Linked to Human Neurological Disease Robert D.S. Pitceathly,1 Shamima Rahman,1,2 Yehani Wedatilake,2 James M. Polke,3 Sebahattin Cirak,5 A. Reghan Foley,5 Anna Sailer,6 Matthew E. Hurles,7 Jim Stalker,7 Iain Hargreaves,4 Cathy E. Woodward,3 Mary G. Sweeney,3 Francesco Muntoni,5 Henry Houlden,1,6 UK10K Consortium, Jan-Willem Taanman,8 and Michael G. Hanna1,6,* 1MRC Centre for Neuromuscular Diseases, UCL Institute of Neurology and National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK 2Mitochondrial Research Group, Clinical and Molecular Genetics Unit, UCL Institute of Child Health, London WC1N 1EH, UK 3Neurogenetics Unit 4Neurometabolic Unit National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK 5Dubowitz Neuromuscular Centre, UCL Institute of Child Health and Great Ormond Street Hospital for Children NHS Foundation Trust, London WC1N 1EH, UK 6Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, UK 7The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK 8Department of Clinical Neuroscience, UCL Institute of Neurology, London NW3 2PF, UK *Correspondence: [email protected] http://dx.doi.org/10.1016/j.celrep.2013.05.005 SUMMARY INTRODUCTION The molecular basis of cytochrome c oxidase (COX, Cytochrome c oxidase (COX, complex IV) is the terminal enzyme complex IV) deficiency remains genetically undeter- complex of the mitochondrial respiratory chain and plays a vital mined in many cases. Homozygosity mapping and role in cellular energy transformation.
    [Show full text]
  • Role of Cytochrome C Oxidase Nuclear-Encoded Subunits in Health and Disease
    Physiol. Res. 69: 947-965, 2020 https://doi.org/10.33549/physiolres.934446 REVIEW Role of Cytochrome c Oxidase Nuclear-Encoded Subunits in Health and Disease Kristýna ČUNÁTOVÁ1, David PAJUELO REGUERA1, Josef HOUŠTĚK1, Tomáš MRÁČEK1, Petr PECINA1 1Department of Bioenergetics, Institute of Physiology, Czech Academy of Sciences, Prague, Czech Republic Received February 2, 2020 Accepted September 13, 2020 Epub Ahead of Print November 2, 2020 Summary [email protected] and Tomáš Mráček, Department of Cytochrome c oxidase (COX), the terminal enzyme of Bioenergetics, Institute of Physiology CAS, Vídeňská 1083, 142 mitochondrial electron transport chain, couples electron transport 20 Prague 4, Czech Republic. E-mail: [email protected] to oxygen with generation of proton gradient indispensable for the production of vast majority of ATP molecules in mammalian Cytochrome c oxidase cells. The review summarizes current knowledge of COX structure and function of nuclear-encoded COX subunits, which may Energy demands of mammalian cells are mainly modulate enzyme activity according to various conditions. covered by ATP synthesis carried out by oxidative Moreover, some nuclear-encoded subunits possess tissue-specific phosphorylation apparatus (OXPHOS) located in the and development-specific isoforms, possibly enabling fine-tuning central bioenergetic organelle, mitochondria. OXPHOS is of COX function in individual tissues. The importance of nuclear- composed of five multi-subunit complexes embedded in encoded subunits is emphasized by recently discovered the inner mitochondrial membrane (IMM). Electron pathogenic mutations in patients with severe mitopathies. In transport from reduced substrates of complexes I and II to addition, proteins substoichiometrically associated with COX were cytochrome c oxidase (COX, complex IV, CIV) is found to contribute to COX activity regulation and stabilization of achieved by increasing redox potential of individual the respiratory supercomplexes.
    [Show full text]
  • WO 2017/070647 Al 27 April 2017 (27.04.2017) P O P C T
    (12) INTERNATIONAL APPLICATION PUBLISHED UNDER THE PATENT COOPERATION TREATY (PCT) (19) World Intellectual Property Organization International Bureau (10) International Publication Number (43) International Publication Date WO 2017/070647 Al 27 April 2017 (27.04.2017) P O P C T (51) International Patent Classification: HN, HR, HU, ID, IL, IN, IR, IS, JP, KE, KG, KN, KP, KR, A61K 31/455 (2006.01) C12N 15/86 (2006.01) KW, KZ, LA, LC, LK, LR, LS, LU, LY, MA, MD, ME, A61K 31/465 (2006.01) A61P 27/02 (2006.01) MG, MK, MN, MW, MX, MY, MZ, NA, NG, NI, NO, NZ, A61K 31/19 (2006.01) A61P 27/06 (2006.01) OM, PA, PE, PG, PH, PL, PT, QA, RO, RS, RU, RW, SA, A61K 48/00 (2006.01) A61K 45/06 (2006.01) SC, SD, SE, SG, SK, SL, SM, ST, SV, SY, TH, TJ, TM, TN, TR, TT, TZ, UA, UG, US, UZ, VC, VN, ZA, ZM, (21) International Application Number: ZW. PCT/US2016/058388 (84) Designated States (unless otherwise indicated, for every (22) International Filing Date: kind of regional protection available): ARIPO (BW, GH, 24 October 2016 (24.10.201 6) GM, KE, LR, LS, MW, MZ, NA, RW, SD, SL, ST, SZ, (25) Filing Language: English TZ, UG, ZM, ZW), Eurasian (AM, AZ, BY, KG, KZ, RU, TJ, TM), European (AL, AT, BE, BG, CH, CY, CZ, DE, (26) Publication Language: English DK, EE, ES, FI, FR, GB, GR, HR, HU, IE, IS, IT, LT, LU, (30) Priority Data: LV, MC, MK, MT, NL, NO, PL, PT, RO, RS, SE, SI, SK, 62/245,467 23 October 2015 (23.
    [Show full text]
  • DJ-1 Binds to Mitochondrial Complex I and Maintains Its Activity
    Title DJ-1 binds to mitochondrial complex I and maintains its activity Hayashi, Takuya; Ishimori, Chikako; Takahashi-Niki, Kazuko; Taira, Takahiro; Kim, Yun-chul; Maita, Hiroshi; Maita, Author(s) Chinatsu; Ariga, Hiroyoshi; Iguchi-Ariga, Sanae M. M. Biochemical and Biophysical Research Communications, 390(3), 667-672 Citation https://doi.org/10.1016/j.bbrc.2009.10.025 Issue Date 2009-12-18 Doc URL http://hdl.handle.net/2115/42484 Type article (author version) File Information BBRC390-3_667-672.pdf Instructions for use Hokkaido University Collection of Scholarly and Academic Papers : HUSCAP *Manuscript DJ-1 binds to mitochondrial complex I and maintains its activity Takuya Hayashia, Chikako Ishimoria, Kazuko Takahashi-Nikic, Takahiro Tairab, Yun-chul Kimc, Hiroshi Maitac, Chinatsu Maitaa, Hiroyoshi Arigac, *, Sanae M.M. Iguchi-Arigaa aGraduate School of Agriculture, Hokkaido University, Sapporo 060-8589, Japan bInterdisciplinary Graduate School of Medicine and Engineering, Yamanashi University, Chuoh, 409-3898, Japan cGraduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan *Correspondence author. Address: Graduate School of Pharmaceutical Sciences, Hokkaido University, Sapporo 060-0812, Japan. Fax: +81 11 706 3745. E-mail address: [email protected] (H. Ariga) 1 ABSTRACT Parkinson’s disease (PD) is caused by neuronal cell death, and oxidative stress and mitochondrial dysfunction are thought to be responsible for onset of PD. DJ-1, a causative gene product of a familial form of Parkinson’s disease, PARK7, plays roles in transcriptional regulation and anti-oxidative stress. The possible mitochondrial function of DJ-1 has been proposed, but its exact function remains unclear. In this study, we found that DJ-1 directly bound to NDUFA4 and ND1, nuclear and mitochondrial DNA-encoding subunits of mitochondrial complex I, respectively, and was co-localized with complex I and that complex I activity was reduced in DJ-1-knockdown NIH3T3 and HEK293cells.
    [Show full text]
  • Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces Cerevisiae
    life Review Human Mitochondrial Pathologies of the Respiratory Chain and ATP Synthase: Contributions from Studies of Saccharomyces cerevisiae Leticia V. R. Franco 1,2,* , Luca Bremner 1 and Mario H. Barros 2 1 Department of Biological Sciences, Columbia University, New York, NY 10027, USA; [email protected] 2 Department of Microbiology,Institute of Biomedical Sciences, Universidade de Sao Paulo, Sao Paulo 05508-900, Brazil; [email protected] * Correspondence: [email protected] Received: 27 October 2020; Accepted: 19 November 2020; Published: 23 November 2020 Abstract: The ease with which the unicellular yeast Saccharomyces cerevisiae can be manipulated genetically and biochemically has established this organism as a good model for the study of human mitochondrial diseases. The combined use of biochemical and molecular genetic tools has been instrumental in elucidating the functions of numerous yeast nuclear gene products with human homologs that affect a large number of metabolic and biological processes, including those housed in mitochondria. These include structural and catalytic subunits of enzymes and protein factors that impinge on the biogenesis of the respiratory chain. This article will review what is currently known about the genetics and clinical phenotypes of mitochondrial diseases of the respiratory chain and ATP synthase, with special emphasis on the contribution of information gained from pet mutants with mutations in nuclear genes that impair mitochondrial respiration. Our intent is to provide the yeast mitochondrial specialist with basic knowledge of human mitochondrial pathologies and the human specialist with information on how genes that directly and indirectly affect respiration were identified and characterized in yeast. Keywords: mitochondrial diseases; respiratory chain; yeast; Saccharomyces cerevisiae; pet mutants 1.
    [Show full text]
  • Influenza-Specific Effector Memory B Cells Predict Long-Lived Antibody Responses to Vaccination in Humans
    bioRxiv preprint doi: https://doi.org/10.1101/643973; this version posted February 18, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Influenza-specific effector memory B cells predict long-lived antibody responses to vaccination in humans Anoma Nellore1, Esther Zumaquero2, Christopher D. Scharer3, Rodney G. King2, Christopher M. Tipton4, Christopher F. Fucile5, Tian Mi3, Betty Mousseau2, John E. Bradley6, Fen Zhou2, Paul A. Goepfert1, Jeremy M. Boss3, Troy D. Randall6, Ignacio Sanz4, Alexander F. Rosenberg2,5, Frances E. Lund2 1Dept. of Medicine, Division of Infectious Disease, 2Dept of Microbiology, 5Informatics Institute, 6Dept. of Medicine, Division of Clinical Immunology and Rheumatology and at The University of Alabama at Birmingham, Birmingham, AL 35294 USA 3Dept. of Microbiology and Immunology and 4Department of Medicine, Division of Rheumatology Emory University, Atlanta, GA 30322, USA Correspondence should be addressed to: Frances E. Lund, PhD Charles H. McCauley Professor and Chair Dept of Microbiology University of Alabama at Birmingham 276 BBRB Box 11 1720 2nd Avenue South Birmingham AL 35294-2170 [email protected] SHORT RUNNING TITLE: Effector memory B cell development after influenza vaccination 1 bioRxiv preprint doi: https://doi.org/10.1101/643973; this version posted February 18, 2021. The copyright holder for this preprint (which was not certified by peer review) is the author/funder. All rights reserved. No reuse allowed without permission. Abstract Seasonal influenza vaccination elicits hemagglutinin (HA)-specific CD27+ memory B cells (Bmem) that differ in expression of T-bet, BACH2 and TCF7.
    [Show full text]
  • NDUFA4 Mutations Underlie Dysfunction of a Cytochrome C Oxidase Subunit Linked to Human Neurological Disease
    Cell Reports Report NDUFA4 Mutations Underlie Dysfunction of a Cytochrome c Oxidase Subunit Linked to Human Neurological Disease Robert D.S. Pitceathly,1 Shamima Rahman,1,2 Yehani Wedatilake,2 James M. Polke,3 Sebahattin Cirak,5 A. Reghan Foley,5 Anna Sailer,6 Matthew E. Hurles,7 Jim Stalker,7 Iain Hargreaves,4 Cathy E. Woodward,3 Mary G. Sweeney,3 Francesco Muntoni,5 Henry Houlden,1,6 UK10K Consortium, Jan-Willem Taanman,8 and Michael G. Hanna1,6,* 1MRC Centre for Neuromuscular Diseases, UCL Institute of Neurology and National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK 2Mitochondrial Research Group, Clinical and Molecular Genetics Unit, UCL Institute of Child Health, London WC1N 1EH, UK 3Neurogenetics Unit 4Neurometabolic Unit National Hospital for Neurology and Neurosurgery, Queen Square, London WC1N 3BG, UK 5Dubowitz Neuromuscular Centre, UCL Institute of Child Health and Great Ormond Street Hospital for Children NHS Foundation Trust, London WC1N 1EH, UK 6Department of Molecular Neuroscience, UCL Institute of Neurology, Queen Square, London WC1N 3BG, UK 7The Wellcome Trust Sanger Institute, Wellcome Trust Genome Campus, Hinxton, Cambridge CB10 1SA, UK 8Department of Clinical Neuroscience, UCL Institute of Neurology, London NW3 2PF, UK *Correspondence: [email protected] http://dx.doi.org/10.1016/j.celrep.2013.05.005 SUMMARY INTRODUCTION The molecular basis of cytochrome c oxidase (COX, Cytochrome c oxidase (COX, complex IV) is the terminal enzyme complex IV) deficiency remains genetically undeter- complex of the mitochondrial respiratory chain and plays a vital mined in many cases. Homozygosity mapping and role in cellular energy transformation.
    [Show full text]
  • Multiple Mechanisms Regulate Eukaryotic Cytochrome C Oxidase
    cells Review Multiple Mechanisms Regulate Eukaryotic Cytochrome C Oxidase Rabia Ramzan 1, Bernhard Kadenbach 2,* and Sebastian Vogt 3 1 Cardiovascular Research Laboratory, Biochemical-Pharmacological Center, Philipps-University Marburg, Karl-von-Frisch-Strasse 1, D-35043 Marburg, Germany; [email protected] 2 Fachbereich Chemie, Philipps-University, D-35032 Marburg, Germany 3 Department of Heart Surgery, Campus Marburg, University Hospital of Giessen and Marburg, D-35043 Marburg, Germany; [email protected] * Correspondence: [email protected] Abstract: Cytochrome c oxidase (COX), the rate-limiting enzyme of mitochondrial respiration, is regulated by various mechanisms. Its regulation by ATP (adenosine triphosphate) appears of particular importance, since it evolved early during evolution and is still found in cyanobacteria, but not in other bacteria. Therefore the “allosteric ATP inhibition of COX” is described here in more detail. Most regulatory properties of COX are related to “supernumerary” subunits, which are largely absent in bacterial COX. The “allosteric ATP inhibition of COX” was also recently described in intact isolated rat heart mitochondria. Keywords: mitochondria; energy metabolism; respiration; regulation; cytochrome c oxidase; adenine nucleotides; electron transport; efficiency; ROS generation 1. Introduction Citation: Ramzan, R.; Kadenbach, B.; There exists a basic difference in the regulation of ATP synthesis by oxidative phospho- Vogt, S. Multiple Mechanisms rylation (OxPhos) between bacteria (except cyanobacteria) and eukaryotic organisms. Aer- Regulate Eukaryotic Cytochrome C obic bacteria grow and divide continuously under constant conditions. Higher organisms Oxidase. Cells 2021, 10, 514. https:// change the rates of ATP synthesis and consumption up to a factor of 10 depending on vari- doi.org/10.3390/cells10030514 ous inner and outer signals.
    [Show full text]