The NDUFB1 gene, located on the q arm of chromosome 14 in position 32.12, is 5,687 base pairs long. The NDUFB1 protein weighs 7 kDa and is composed of 58 amino acids.[7][8] NDUFB1 is a subunit of the enzyme NADH dehydrogenase (ubiquinone), the largest of the respiratory complexes. The structure is L-shaped with a long, hydrophobictransmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site.[6] NDUFB1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I. It has been noted that the N-terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C-terminal hydrophilic domain interacting with globular subunits of Complex I. The highly conserved two-domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase (ubiquinone) complex at the inner mitochondrial membrane.[5]
Functionedit
The human NDUFB1 gene codes for a subunit of Complex I of the respiratory chain, which transfers electrons from NADH to ubiquinone.[5] However, NDUFB1 is an accessory subunit of the complex that is believed not to be involved in catalysis.[9] Initially, NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide (FMN) prosthetic arm to form FMNH2. The electrons are transferred through a series of iron-sulfur (Fe-S) clusters in the prosthetic arm and finally to coenzyme Q10 (CoQ), which is reduced to ubiquinol (CoQH2). The flow of electrons changes the redox state of the protein, resulting in a conformational change and pK shift of the ionizable side chain, which pumps four hydrogen ions out of the mitochondrial matrix.[6]
Referencesedit
^ abcGRCh38: Ensembl release 89: ENSG00000183648 - Ensembl, May 2017
^"Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^"Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^Emahazion T, Beskow A, Gyllensten U, Brookes AJ (Nov 1998). "Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain". Cytogenet Cell Genet. 82 (1–2): 115–9. doi:10.1159/000015082. PMID 9763677. S2CID 46818955.
^ abcVoet D, Voet JG, Pratt CW (2013). "Chapter 18". Fundamentals of biochemistry: life at the molecular level (4th ed.). Hoboken, NJ: Wiley. pp. 581–620. ISBN978-0-470-54784-7.
^Zong NC, Li H, Li H, Lam MP, Jimenez RC, Kim CS, Deng N, Kim AK, Choi JH, Zelaya I, Liem D, Meyer D, Odeberg J, Fang C, Lu HJ, Xu T, Weiss J, Duan H, Uhlen M, Yates JR, Apweiler R, Ge J, Hermjakob H, Ping P (Oct 2013). "Integration of cardiac proteome biology and medicine by a specialized knowledgebase". Circulation Research. 113 (9): 1043–53. doi:10.1161/CIRCRESAHA.113.301151. PMC4076475. PMID 23965338.
^"NDUFB1 - NADH dehydrogenase [ubiquinone] 1 beta subcomplex subunit 1". UniProt: a hub for protein information. The UniProt Consortium. Retrieved 2 April 2015.
Further readingedit
Rual JF, Venkatesan K, Hao T, et al. (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
Gerhard DS, Wagner L, Feingold EA, et al. (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC528928. PMID 15489334.
Strausberg RL, Feingold EA, Grouse LH, et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC139241. PMID 12477932.
Zhang QH, Ye M, Wu XY, et al. (2001). "Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34+ hematopoietic stem/progenitor cells". Genome Res. 10 (10): 1546–60. doi:10.1101/gr.140200. PMC310934. PMID 11042152.
Loeffen JL, Triepels RH, van den Heuvel LP, et al. (1999). "cDNA of eight nuclear encoded subunits of NADH:ubiquinone oxidoreductase: human complex I cDNA characterization completed". Biochem. Biophys. Res. Commun. 253 (2): 415–22. doi:10.1006/bbrc.1998.9786. PMID 9878551.
Mao M, Fu G, Wu JS, et al. (1998). "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning". Proc. Natl. Acad. Sci. U.S.A. 95 (14): 8175–80. Bibcode:1998PNAS...95.8175M. doi:10.1073/pnas.95.14.8175. PMC20949. PMID 9653160.
Ton C, Hwang DM, Dempsey AA, Liew CC (1998). "Identification and primary structure of five human NADH-ubiquinone oxidoreductase subunits". Biochem. Biophys. Res. Commun. 241 (2): 589–94. doi:10.1006/bbrc.1997.7707. PMID 9425316.
ndufb1, nadh, dehydrogenase, ubiquinone, beta, subcomplex, subunit, enzyme, that, humans, encoded, gene, nadh, dehydrogenase, ubiquinone, beta, subcomplex, 7kda, accessory, subunit, nadh, dehydrogenase, ubiquinone, complex, located, mitochondrial, inner, membr. NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 1 is an enzyme that in humans is encoded by the NDUFB1 gene 4 5 NADH dehydrogenase ubiquinone 1 beta subcomplex 1 7kDa is an accessory subunit of the NADH dehydrogenase ubiquinone complex located in the mitochondrial inner membrane It is also known as Complex I and is the largest of the five complexes of the electron transport chain 6 NDUFB1IdentifiersAliasesNDUFB1 CI MNLL CI SGDH MNLL NADH ubiquinone oxidoreductase subunit B1External IDsOMIM 603837 HomoloGene 129534 GeneCards NDUFB1Gene location Human Chr Chromosome 14 human 1 Band14q32 12Start92 116 122 bp 1 End92 121 917 bp 1 RNA expression patternBgeeHumanMouse ortholog Top expressed inleft ventricleright ventriclerenal medullaanterior pituitaryendothelial cellbody of tonguenucleus accumbensbiceps brachiiAchilles tendoncaudate nucleusn aMore reference expression dataBioGPSMore reference expression dataGene ontologyMolecular functionNADH dehydrogenase ubiquinone activity NADH dehydrogenase activityCellular componentintegral component of membrane mitochondrial inner membrane mitochondrial respiratory chain complex I respirasome membrane mitochondrion nuclear speckBiological processmitochondrial electron transport NADH to ubiquinone mitochondrial respiratory chain complex I assemblySources Amigo QuickGOOrthologsSpeciesHumanMouseEntrez4707102631912EnsemblENSG00000183648n aUniProtO75438n aRefSeq mRNA NM 004545n aRefSeq protein NP 004536n aLocation UCSC Chr 14 92 12 92 12 Mbn aPubMed search 2 3 WikidataView Edit HumanView Edit Mouse Contents 1 Structure 2 Function 3 References 4 Further readingStructure editThe NDUFB1 gene located on the q arm of chromosome 14 in position 32 12 is 5 687 base pairs long The NDUFB1 protein weighs 7 kDa and is composed of 58 amino acids 7 8 NDUFB1 is a subunit of the enzyme NADH dehydrogenase ubiquinone the largest of the respiratory complexes The structure is L shaped with a long hydrophobic transmembrane domain and a hydrophilic domain for the peripheral arm that includes all the known redox centers and the NADH binding site 6 NDUFB1 is one of about 31 hydrophobic subunits that form the transmembrane region of Complex I It has been noted that the N terminal hydrophobic domain has the potential to be folded into an alpha helix spanning the inner mitochondrial membrane with a C terminal hydrophilic domain interacting with globular subunits of Complex I The highly conserved two domain structure suggests that this feature is critical for the protein function and that the hydrophobic domain acts as an anchor for the NADH dehydrogenase ubiquinone complex at the inner mitochondrial membrane 5 Function editThe human NDUFB1 gene codes for a subunit of Complex I of the respiratory chain which transfers electrons from NADH to ubiquinone 5 However NDUFB1 is an accessory subunit of the complex that is believed not to be involved in catalysis 9 Initially NADH binds to Complex I and transfers two electrons to the isoalloxazine ring of the flavin mononucleotide FMN prosthetic arm to form FMNH2 The electrons are transferred through a series of iron sulfur Fe S clusters in the prosthetic arm and finally to coenzyme Q10 CoQ which is reduced to ubiquinol CoQH2 The flow of electrons changes the redox state of the protein resulting in a conformational change and pK shift of the ionizable side chain which pumps four hydrogen ions out of the mitochondrial matrix 6 References edit a b c GRCh38 Ensembl release 89 ENSG00000183648 Ensembl May 2017 Human PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Mouse PubMed Reference National Center for Biotechnology Information U S National Library of Medicine Emahazion T Beskow A Gyllensten U Brookes AJ Nov 1998 Intron based radiation hybrid mapping of 15 complex I genes of the human electron transport chain Cytogenet Cell Genet 82 1 2 115 9 doi 10 1159 000015082 PMID 9763677 S2CID 46818955 a b c Entrez Gene NDUFB1 NADH dehydrogenase ubiquinone 1 beta subcomplex 1 7kDa a b c Voet D Voet JG Pratt CW 2013 Chapter 18 Fundamentals of biochemistry life at the molecular level 4th ed Hoboken NJ Wiley pp 581 620 ISBN 978 0 470 54784 7 Zong NC Li H Li H Lam MP Jimenez RC Kim CS Deng N Kim AK Choi JH Zelaya I Liem D Meyer D Odeberg J Fang C Lu HJ Xu T Weiss J Duan H Uhlen M Yates JR Apweiler R Ge J Hermjakob H Ping P Oct 2013 Integration of cardiac proteome biology and medicine by a specialized knowledgebase Circulation Research 113 9 1043 53 doi 10 1161 CIRCRESAHA 113 301151 PMC 4076475 PMID 23965338 NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 1 Cardiac Organellar Protein Atlas Knowledgebase COPaKB NDUFB1 NADH dehydrogenase ubiquinone 1 beta subcomplex subunit 1 UniProt a hub for protein information The UniProt Consortium Retrieved 2 April 2015 Further reading editRual JF Venkatesan K Hao T et al 2005 Towards a proteome scale map of the human protein protein interaction network Nature 437 7062 1173 8 Bibcode 2005Natur 437 1173R doi 10 1038 nature04209 PMID 16189514 S2CID 4427026 Gerhard DS Wagner L Feingold EA et al 2004 The status quality and expansion of the NIH full length cDNA project the Mammalian Gene Collection MGC Genome Res 14 10B 2121 7 doi 10 1101 gr 2596504 PMC 528928 PMID 15489334 Strausberg RL Feingold EA Grouse LH et al 2003 Generation and initial analysis of more than 15 000 full length human and mouse cDNA sequences Proc Natl Acad Sci U S A 99 26 16899 903 Bibcode 2002PNAS 9916899M doi 10 1073 pnas 242603899 PMC 139241 PMID 12477932 Zhang QH Ye M Wu XY et al 2001 Cloning and functional analysis of cDNAs with open reading frames for 300 previously undefined genes expressed in CD34 hematopoietic stem progenitor cells Genome Res 10 10 1546 60 doi 10 1101 gr 140200 PMC 310934 PMID 11042152 Loeffen JL Triepels RH van den Heuvel LP et al 1999 cDNA of eight nuclear encoded subunits of NADH ubiquinone oxidoreductase human complex I cDNA characterization completed Biochem Biophys Res Commun 253 2 415 22 doi 10 1006 bbrc 1998 9786 PMID 9878551 Mao M Fu G Wu JS et al 1998 Identification of genes expressed in human CD34 hematopoietic stem progenitor cells by expressed sequence tags and efficient full length cDNA cloning Proc Natl Acad Sci U S A 95 14 8175 80 Bibcode 1998PNAS 95 8175M doi 10 1073 pnas 95 14 8175 PMC 20949 PMID 9653160 Ton C Hwang DM Dempsey AA Liew CC 1998 Identification and primary structure of five human NADH ubiquinone oxidoreductase subunits Biochem Biophys Res Commun 241 2 589 94 doi 10 1006 bbrc 1997 7707 PMID 9425316 This article incorporates text from the United States National Library of Medicine which is in the public domain Retrieved from https en wikipedia org w index php title NDUFB1 amp oldid 1142674902, wikipedia, wiki, book, books, library,
