Substrate-induced conformational change in bacterial complex I.
about
Redox-dependent change of nucleotide affinity to the active site of the mammalian complex IStructural Basis for the Mechanism of Respiratory Complex IThe architecture of respiratory complex IA cytochrome c fusion protein domain for convenient detection, quantification, and enhanced production of membrane proteins in Escherichia coli--expression and characterization of cytochrome-tagged Complex I subunitsSulfo-SMCC Prevents Annealing of Taxol-Stabilized Microtubules In VitroTowards the molecular mechanism of respiratory complex I.Kinetics and regulation of mammalian NADH-ubiquinone oxidoreductase (Complex I).Evolution of respiratory complex I: "supernumerary" subunits are present in the alpha-proteobacterial enzyme.A giant molecular proton pump: structure and mechanism of respiratory complex I.Synthesis and characterization of new piperazine-type inhibitors for mitochondrial NADH-ubiquinone oxidoreductase (complex I).Geometric and electrostatic study of the [4Fe-4S] cluster of adenosine-5'-phosphosulfate reductase from broken symmetry density functional calculations and extended X-ray absorption fine structure spectroscopy.Definition of the mitochondrial proteome by measurement of molecular masses of membrane proteins.Structural contribution of C-terminal segments of NuoL (ND5) and NuoM (ND4) subunits of complex I from Escherichia coli.Substrate recognition, protein dynamics, and iron-sulfur cluster in Pseudomonas aeruginosa adenosine 5'-phosphosulfate reductase.Mitochondrial respiratory complex I: structure, function and implication in human diseases.Semiquinone and cluster N6 signals in His-tagged proton-translocating NADH:ubiquinone oxidoreductase (complex I) from Escherichia coliNADH/NAD+ interaction with NADH: ubiquinone oxidoreductase (complex I).Architecture of complex I and its implications for electron transfer and proton pumping.The role of proton and sodium ions in energy transduction by respiratory complex I.Characterisation of the active/de-active transition of mitochondrial complex I.Chemical modifications of respiratory complex I for structural and functional studies.Engineering the respiratory complex I to energy-converting NADPH:ubiquinone oxidoreductase.ND3, ND1 and 39kDa subunits are more exposed in the de-active form of bovine mitochondrial complex I.Characterization of the Nqo5 subunit of bacterial complex I in the isolated state.Electrostatics of the FeS clusters in respiratory complex I.The three-dimensional structure of complex I from Yarrowia lipolytica: a highly dynamic enzyme.Reverse electron transfer results in a loss of flavin from mitochondrial complex I: Potential mechanism for brain ischemia reperfusion injury.Probing the proton channels in subunit N of Complex I from Escherichia coli through intra-subunit cross-linking.The Redox-Bohr Group Associated with Iron-Sulfur Cluster N2 of Complex ISuperoxide Radical Formation by Pure Complex I (NADH:Ubiquinone Oxidoreductase) fromYarrowia lipolytica
P2860
Q24642076-2CBDDE81-71B5-448F-9F0C-D4C5466CEA43Q27656732-07C8DBF2-C3A9-4D99-8421-8D570976B90FQ27661963-73E723D7-6193-4167-BAD7-F2C75CCA6643Q28488918-16B9D0F5-9A54-4E80-9513-E17F9DE2FF8AQ28553717-ABB35B5A-87C9-4104-A361-6B6539D77736Q34020648-FAEAD7AA-999A-466E-8C11-1A37D0827301Q34099013-2B9BDA87-2C84-4601-B5E3-75B2B8C4DFDBQ34152292-F5C85062-A78C-4D9F-A631-4821578AA157Q34477041-47770A86-9D67-48B4-974C-4DFA095FB139Q34596917-D578FB0D-3FBF-4B48-9E6B-97A3166956CAQ35098826-642C5CB2-72AE-4CDC-A5CB-23B78393BAA9Q35107347-1362B9B2-9FE7-4EFE-89BB-3C9F34B1D311Q35310865-2DF7D564-273E-45A8-B3D4-7E37FE8925BBQ35585311-32612F77-056B-4EE2-A6A0-1E80FA80304DQ36444688-DB4BF85D-4900-45F5-AD81-180D0C95FDE5Q36850300-341F930F-A612-4941-A3E9-DE93923F91A7Q37159629-10FB268E-E4B4-41E9-A983-7492ED132C10Q37234977-E3DC23ED-D6D9-486C-84BD-F56AC3BEDA76Q38009270-1D51FDDA-1BD8-4C61-A2BD-8C1980614D8BQ38191082-E79F92E8-7337-4B92-B6EE-5EA6FFBEFA38Q38226104-99B3D0ED-28FD-43F7-A6F2-2550CABD1E1BQ38621373-95598321-9EF7-45CD-A755-6E20BB396096Q41875296-29B22F05-70D0-4FEE-818A-86A3F9989DACQ41879839-41443319-4C75-439B-97EF-85F28A216E54Q41945131-14CBA4F9-9A85-4C5D-BF2F-4079F280F695Q43024932-52AA9143-DDE9-447C-A2ED-804D0B5DFA42Q46306550-F344F12E-5F01-4852-AA3A-1D2470DD0A14Q47139010-62F383BC-48BA-49BE-8B22-67FA1CE21500Q58782339-00A04E24-CB8C-41CA-B2EA-A1796F3C47C3Q58782439-E7478655-D7FF-4FCF-926C-7A046E06E05C
P2860
Substrate-induced conformational change in bacterial complex I.
description
2004 nî lūn-bûn
@nan
2004年の論文
@ja
2004年論文
@yue
2004年論文
@zh-hant
2004年論文
@zh-hk
2004年論文
@zh-mo
2004年論文
@zh-tw
2004年论文
@wuu
2004年论文
@zh
2004年论文
@zh-cn
name
Substrate-induced conformational change in bacterial complex I.
@en
Substrate-induced conformational change in bacterial complex I.
@nl
type
label
Substrate-induced conformational change in bacterial complex I.
@en
Substrate-induced conformational change in bacterial complex I.
@nl
prefLabel
Substrate-induced conformational change in bacterial complex I.
@en
Substrate-induced conformational change in bacterial complex I.
@nl
P2093
P2860
P356
P1476
Substrate-induced conformational change in bacterial complex I.
@en
P2093
Aygun A Mamedova
Joe Carroll
Peter J Holt
P2860
P304
23830-23836
P356
10.1074/JBC.M401539200
P407
P577
2004-03-22T00:00:00Z