Movement of the iron-sulfur subunit beyond the ef loop of cytochrome b is required for multiple turnovers of the bc1 complex but not for single turnover Qo site catalysis.
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Tether mutations that restore function and suppress pleiotropic phenotypes of the C. elegans isp-1(qm150) Rieske iron-sulfur proteinPhotoinduced electron transfer between the Rieske iron-sulfur protein and cytochrome c(1) in the Rhodobacter sphaeroides cytochrome bc(1) complex. Effects of pH, temperature, and driving force.Chapter 5 Use of ruthenium photooxidation techniques to study electron transfer in the cytochrome bc1 complex.A robust genetic system for producing heterodimeric native and mutant cytochrome bc(1)Tyrosine triad at the interface between the Rieske iron-sulfur protein, cytochrome c1 and cytochrome c2 in the bc1 complex of Rhodobacter capsulatus.X-Ray absorption studies of Zn2+ binding sites in bacterial, avian, and bovine cytochrome bc1 complexes.Mitochondrial Disease-related Mutation G167P in Cytochrome b of Rhodobacter capsulatus Cytochrome bc1 (S151P in Human) Affects the Equilibrium Distribution of [2Fe-2S] Cluster and Generation of Superoxide.Uncovering the Transmembrane Metal Binding Site of the Novel Bacterial Major Facilitator Superfamily-Type Copper Importer CcoA.Proton translocation by the cytochrome bc1 complexes of phototrophic bacteria: introducing the activated Q-cycle.Recent advances in cytochrome bc(1): inter monomer electronic communication?Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome cPhotoinitiated electron transfer within the Paracoccus denitrificans cytochrome bc1 complex: mobility of the iron-sulfur protein is modulated by the occupant of the Q(o) site.Magnetic interactions sense changes in distance between heme b(L) and the iron-sulfur cluster in cytochrome bc(1).Electronic connection between the quinone and cytochrome C redox pools and its role in regulation of mitochondrial electron transport and redox signalingOn the mechanism of quinol oxidation at the QP site in the cytochrome bc1 complex: studied using mutants lacking cytochrome bL or bH.Across membrane communication between the Q(o) and Q(i) active sites of cytochrome bc(1).Discrimination between two possible reaction sequences that create potential risk of generation of deleterious radicals by cytochrome bc₁. Implications for the mechanism of superoxide production.Effect of mutations in the cytochrome b ef loop on the electron-transfer reactions of the Rieske iron-sulfur protein in the cytochrome bc1 complexBinding dynamics at the quinone reduction (Qi) site influence the equilibrium interactions of the iron sulfur protein and hydroquinone oxidation (Qo) site of the cytochrome bc1 complex.The [2Fe-2S] cluster E(m) as an indicator of the iron-sulfur subunit position in the ubihydroquinone oxidation site of the cytochrome bc1 complex.A pathogenic cytochrome b mutation reveals new interactions between subunits of the mitochondrial bc1 complex.Effect of famoxadone on photoinduced electron transfer between the iron-sulfur center and cytochrome c1 in the cytochrome bc1 complex.Functional insensitivity of the cytochrome b6f complex to structure changes in the hinge region of the Rieske iron-sulfur protein.QO site deficiency can be compensated by extragenic mutations in the hinge region of the iron-sulfur protein in the bc1 complex of Saccharomyces cerevisiae.Effect of H bond removal and changes in the position of the iron-sulphur head domain on the spin-lattice relaxation properties of the [2Fe-2S](2+) Rieske cluster in cytochrome bc(1).PetC1 is the major Rieske iron-sulfur protein in the cytochrome b6f complex of Synechocystis sp. PCC 6803.
P2860
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P2860
Movement of the iron-sulfur subunit beyond the ef loop of cytochrome b is required for multiple turnovers of the bc1 complex but not for single turnover Qo site catalysis.
description
2001 nî lūn-bûn
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2001年の論文
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2001年学术文章
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2001年学术文章
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2001年学术文章
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2001年学术文章
@zh-hans
2001年学术文章
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2001年學術文章
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name
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@en
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@nl
type
label
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@en
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@nl
prefLabel
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@en
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@nl
P2860
P356
P1476
Movement of the iron-sulfur su ...... le turnover Qo site catalysis.
@en
P2093
Elisabeth Darrouzet
Fevzi Daldal
P2860
P304
P356
10.1074/JBC.M107974200
P407
P577
2001-11-13T00:00:00Z