The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b.
about
Perturbation of the Quinone-binding Site of Complex II Alters the Electronic Properties of the Proximal [3Fe-4S] Iron-Sulfur ClusterUbiquinone-binding site mutagenesis reveals the role of mitochondrial complex II in cell death initiationMutagenesis and functional studies with succinate dehydrogenase inhibitors in the wheat pathogen Mycosphaerella graminicolaMutation of the heme axial ligand of Escherichia coli succinate-quinone reductase: implications for heme ligation in mitochondrial complex II from yeastThe quinone-binding and catalytic site of complex II.Out of plane distortions of the heme b of Escherichia coli succinate dehydrogenaseA conserved lysine residue controls iron-sulfur cluster redox chemistry in Escherichia coli fumarate reductase.Metabolic transistor strategy for controlling electron transfer chain activity in Escherichia coliManipulating respiratory levels in Escherichia coli for aerobic formation of reduced chemical products.Escherichia coli succinate dehydrogenase variant lacking the heme b.Structural basis for malfunction in complex II.Catalytic mechanisms of complex II enzymes: a structural perspectiveDefining a direction: electron transfer and catalysis in Escherichia coli complex II enzymes.Alpha-tocopheryl succinate induces apoptosis by targeting ubiquinone-binding sites in mitochondrial respiratory complex II.Electron-transfer pathways in the heme and quinone-binding domain of complex II (succinate dehydrogenase).Mitochondrial respiratory chain complexes: apoptosis sensors mutated in cancer?Inhibitors of succinate: quinone reductase/Complex II regulate production of mitochondrial reactive oxygen species and protect normal cells from ischemic damage but induce specific cancer cell death.Expression of Saccharomyces cerevisiae Sdh3p and Sdh4p paralogs results in catalytically active succinate dehydrogenase isoenzymes.Why hypothetical protein KPN00728 of Klebsiella pneumoniae should be classified as chain C of succinate dehydrogenase?Specific disintegration of complex II succinate:ubiquinone oxidoreductase links pH changes to oxidative stress for apoptosis inductionNovel mitochondrial complex II isolated from Trypanosoma cruzi is composed of 12 peptides including a heterodimeric Ip subunit.Discovering Novel Alternaria solani Succinate Dehydrogenase Inhibitors by in Silico Modeling and Virtual Screening Strategies to Combat Early Blight.Characterisation of Ramularia collo-cygni laboratory mutants resistant to succinate dehydrogenase inhibitors.The antimicrobial action of polyaniline involves production of oxidative stress while functionalisation of polyaniline introduces additional mechanisms.Ubiquinone-binding Site Mutations in theSaccharomyces cerevisiaeSuccinate Dehydrogenase Generate Superoxide and Lead to the Accumulation of Succinate
P2860
Q27666928-6119C7F8-148F-45B6-83BC-756746488C0DQ28395613-6AF8C6CB-229D-4025-96B0-42F54C23B61CQ28730455-E946E709-C94B-48B4-8F9F-32A33DD6FA38Q33926010-C3327062-47CB-4D21-BAD3-C136B83DDBCDQ33937869-62F9F66A-755B-4C6E-ACC9-F3EA6EA9D118Q34185969-74755B96-DA9A-4E0A-8A65-BC06D72F949EQ35162513-92E8BF71-EAFF-44C8-BF8B-17BA514ED72CQ35164149-D248C796-A41F-4644-9E95-2EC8A566FEADQ35535607-F9C991C9-0467-4ED1-8515-F2B86B9B4E80Q36156713-86E2619A-C708-4205-88E4-D5AA37B362F3Q36318828-43A6C118-335C-4373-B1F5-7E8540EFD886Q36511118-A51C5260-17C9-4C91-89B3-2FC804D09492Q36736109-86C9BADE-FB78-4390-AAA8-C44DB7B41E20Q37158312-1E46EE08-A76A-43CF-A411-A5A0E71BFD33Q37701708-C970B4D5-6314-417C-B0DF-ED750CF6D297Q37882392-FE5AC291-873E-424A-B99D-C54782FBDCF4Q37921677-2BF4869F-35A9-437A-9769-A005427DD3EDQ41830350-952A83B0-2E19-4BBE-9107-D29678FB4C25Q42099630-893F6A74-AF3A-4635-8876-E98DDA67536DQ42630202-88F0CFFD-ACC6-468E-A1EB-861883D04CA6Q43167112-A875B036-8C95-4275-80B7-4D70FA03A6E7Q48581596-2D6E3FF3-1B51-4A42-BE69-5884243ED93EQ51490464-DA09AC18-0EA8-4BAD-8CF7-D85F27DA34A6Q55438177-FACEC376-E7CC-4CDA-9497-0EA9AE4E7965Q57658444-75A79E0F-9259-4D53-8E82-0EC6172BD532
P2860
The quinone binding site in Escherichia coli succinate dehydrogenase is required for electron transfer to the heme b.
description
2006 nî lūn-bûn
@nan
2006 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2006 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2006年の論文
@ja
2006年学术文章
@wuu
2006年学术文章
@zh-cn
2006年学术文章
@zh-hans
2006年学术文章
@zh-my
2006年学术文章
@zh-sg
2006年學術文章
@yue
name
The quinone binding site in Es ...... ectron transfer to the heme b.
@ast
The quinone binding site in Es ...... ectron transfer to the heme b.
@en
The quinone binding site in Es ...... ectron transfer to the heme b.
@nl
type
label
The quinone binding site in Es ...... ectron transfer to the heme b.
@ast
The quinone binding site in Es ...... ectron transfer to the heme b.
@en
The quinone binding site in Es ...... ectron transfer to the heme b.
@nl
prefLabel
The quinone binding site in Es ...... ectron transfer to the heme b.
@ast
The quinone binding site in Es ...... ectron transfer to the heme b.
@en
The quinone binding site in Es ...... ectron transfer to the heme b.
@nl
P2093
P2860
P356
P1476
The quinone binding site in Es ...... lectron transfer to the heme b
@en
P2093
Elena Maklashina
Gary Cecchini
Joel H Weiner
Quang M Tran
P2860
P304
32310-32317
P356
10.1074/JBC.M607476200
P407
P577
2006-09-01T00:00:00Z