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Direct assignment of EPR spectra to structurally defined iron-sulfur clusters in complex I by double electron-electron resonanceBinding of histidine in the (Cys)3(His)1-coordinated [2Fe-2S] cluster of human mitoNEET.Site-directed mutagenesis of conserved cysteine residues in Escherichia coli fumarate reductase: modification of the spectroscopic and electrochemical properties of the [2Fe-2S] cluster.Electron paramagnetic resonance determination of a low-lying excited state in Chromatium vinosum high-potential iron protein.Advanced paramagnetic resonance spectroscopies of iron-sulfur proteins: Electron nuclear double resonance (ENDOR) and electron spin echo envelope modulation (ESEEM)Mossbauer spectroscopy of the iron-sulfur proteinsThe number of iron atoms in the paramagnetic center (G =1.94) of reduced putidaredoxin, a nonheme iron protein.Mössbauer studies on putidaredoxin.Magnetic resonance of membranes.Lessons from Nature: A Bio-Inspired Approach to Molecular Design.Tetrahedral iron in the active center of plant ferredoxins and beef adrenodoxin.Proton magnetic resonance studies of the ferredoxins from spinach and parsley.Iron in evolution.Metal ion oxidation state assignment based on coordinating ligand hyperfine interaction.Mössbauer evidence on the form of iron in xanthine oxidase.Spectroscopic studies on two-iron ferredoxins.The properties of the primary electron acceptor in the Photosystem I reaction centre of spinach chloroplasts and its interaction with P700 and the bound ferredoxin in various oxidation-reduction statesMössbauer spectroscopy on respiratory complex I: the iron-sulfur cluster ensemble in the NADH-reduced enzyme is partially oxidized.The stoicheiometry of electron transfer by bacterial and plant ferredoxins.Mössbauer effect in the eight-iron ferredoxin from Clostridium pasterurianum. Evidence for the state of the iron atomsThe redox potentials of the two-iron plant and algal ferredoxins. An electrostatic model.Mössbauer effect in Scenedesmus and spinach ferredoxins. The mechanism of electron transfer in plant-type iron-sulphur proteinsLooking at enzymes in action in the 1950s.The state of the iron atoms in hydroxylase iron-sulphur proteins.Spectroscopic characterization of ferredoxin from the blue-green alga Microcystis flos-aquae.Mössbauer effect in rubredoxin. Determination of the hyperfine field of the iron in a simple iron-sulphur protein.The reduced [2Fe-2S] clusters in adrenodoxin and Arthrospira platensis ferredoxin share spin density with protein nitrogens, probed using 2D ESEEM.Analysis of the high-spin states of the 2[4Fe-4Se]+ ferredoxin from Clostridium pasteurianum by Mössbauer spectroscopy.The orientation of iron-sulphur clusters in membrane multilayers prepared from aerobically-grown Escherichia coli K12 and a cytochrome-deficient mutant.Mössbauer studies of adrenodoxin. The mechanism of electron transfer in a hydroxylase iron-sulphur protein.ISC-like [2Fe-2S] ferredoxin (FdxB) dimer from Pseudomonas putida JCM 20004: structural and electron-nuclear double resonance characterization.Low-energy spectrum of iron-sulfur clusters directly from many-particle quantum mechanics.EPR spectroscopy of complex biological iron-sulfur systems.The possible structural and functional role of aromatic residues in bacterial ferredoxins.RsmA is an anti-sigma factor that modulates its activity through a [2Fe-2S] cluster cofactor.
P2860
Q24645274-DD2B40E5-A084-4F57-9585-8EBAB39BE887Q33645749-37AFC40C-5892-4588-A1AC-DE0EC813BF74Q33899818-CFBBBCFD-44D1-4350-884E-E5BCF758C007Q34655966-DC0C4AD5-FC91-4C1D-B016-1AB80DEF6093Q35329323-5200E897-E6CE-4C4E-8285-13394A9688B1Q36447335-C74E7A65-D534-4C74-8917-4E4BC6F56C70Q36469421-4AC9AB4A-1E77-427E-B34F-3CE065E12390Q36470376-A39E6311-6BEC-49D6-A039-69EE384CC9FCQ37169304-06211542-195F-47BC-B70C-6E46F59223F8Q37396593-65F3F63E-186F-4215-8F2B-9AB1269AE3F8Q37493755-05A6399A-3A84-4C09-95AF-12FB0206ABD4Q37545367-7C27B50E-C9C3-4D86-BD18-597469F6B241Q37894282-ECC31611-D141-428E-A028-E007EF1CDE2CQ38348656-3E763135-9179-46CE-BE70-314F81180DE1Q39267047-E002DB60-68DA-4EF9-B8E7-E21C0D36B026Q39903606-757B493B-F630-4A80-A598-897555DA9867Q40013565-EC37ED18-2520-4D29-A71B-AEC775B42FADQ40259701-CA8D41F8-D221-404D-8D38-AA6E41D31D7BQ41836906-F4E21280-236B-4F2D-B143-C8931E4F0959Q41920278-73B82909-4A3A-4B2D-8E58-70E4FB0AC456Q42012204-A0E7AB88-C4BA-43D7-AB71-34377720D0B3Q42018836-EDBCF129-BF82-4BB3-AE4C-30DA1610C36DQ42045057-D4D05AD1-4CEE-4EE2-8626-28BA83A6ADD6Q42053441-FEC4A0F3-AF04-495B-B893-E0E806672F99Q42126214-79B99865-5327-4DFD-9DC4-4F976A064727Q42147919-6BC604C9-A3BB-449D-A053-B4C17274C9E0Q42615551-4F61A911-1F89-4E08-A88A-777346725A94Q42855556-F0BAEC89-2897-4895-926B-FCB2826818F0Q42881351-86873319-B2D8-4823-B3EB-14369A15CDFAQ42924353-362A18D1-8E75-4E06-BFEC-0263072BBBBDQ45184544-8D7D7F8F-6D29-4EEF-9D3A-FE2116A81FD0Q51696359-702E00D9-C5A0-47BF-BA98-3456F2E6D4AAQ52375013-24C22389-5CDE-4F3F-A0BD-30BC093FB464Q52926599-018CDA19-9A2D-41AC-BE07-5CD05ACB2401Q54435187-6EF2F6D8-02D6-4668-9C5A-B5742F79BC41
P2860
description
1966 nî lūn-bûn
@nan
1966年の論文
@ja
1966年学术文章
@wuu
1966年学术文章
@zh-cn
1966年学术文章
@zh-hans
1966年学术文章
@zh-my
1966年学术文章
@zh-sg
1966年學術文章
@yue
1966年學術文章
@zh
1966年學術文章
@zh-hant
name
The iron complex in spinach ferredoxin.
@ast
The iron complex in spinach ferredoxin.
@en
type
label
The iron complex in spinach ferredoxin.
@ast
The iron complex in spinach ferredoxin.
@en
prefLabel
The iron complex in spinach ferredoxin.
@ast
The iron complex in spinach ferredoxin.
@en
P2093
P2860
P356
P1476
The iron complex in spinach ferredoxin.
@en
P2093
F R Whatley
J F Gibson
J H Thornley
P2860
P304
P356
10.1073/PNAS.56.3.987
P407
P577
1966-09-01T00:00:00Z