Interaction between cytochrome c and ubiquinone-cytochrome c oxidoreductase: A study with water-soluble carbodiimides

Gutweniger, Heidi; Grassi, Cristina; Bisson, Roberto

doi:10.1016/0006-291x(83)90411-4

Cited by 23 publications

(11 citation statements)

References 42 publications

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“…Extensive chemical modification studies have demonstrated that six lysine amino groups surrounding the heme crevice of C c are involved in binding to cyt bc 1 [93-96]. Chemical modification and cross-linking studies have shown that acidic residues on cyt c 1 and subunit 8 in bovine cyt bc 1 are involved in binding C c [97, 98]. X-ray crystal structures of beef, chicken, yeast, and R. sphaeroides cyt bc 1 reveal that the cyt c 1 heme edge on the cytoplasmic surface is surrounded by acidic residues that could form a binding site for C c [5-9].…”

Section: Reaction Between Cytochrome Bc1 and Cytochrome Cmentioning

confidence: 99%

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c

Millett

Havens

Rajagukguk

et al. 2013

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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The cytochrome bc1 complex (ubiquinone:cytochrome c oxidoreductase) is the central integral membrane protein in the mitochondrial respiratory chain as well as the electron-transfer chains of many respiratory and photosynthetic prokaryotes. Based on X-ray crystallographic studies of cytochrome bc1, a mechanism has been proposed in which the extrinsic domain of the iron-sulfur protein first binds to cytochrome b where it accepts an electron from ubiquinol in the Qo site, and then rotates by 57o to a position close to cytochrome c1 where it transfers an electron to cytochrome c1. This review describes the development of a ruthenium photooxidation technique to measure key electron transfer steps in cytochrome bc1, including rapid electron transfer from the iron-sulfur protein to cytochrome c1. It was discovered that this reaction is rate-limited by the rotational dynamics of the iron-sulfur protein rather than true electron transfer. A conformational linkage between the occupant of the Qo ubiquinol binding site and the rotational dynamics of the iron-sulfur protein was discovered which could play a role in the bifurcated oxidation of ubiquinol. A ruthenium photoexcitation method is also described for the measurement of electron transfer from cytochrome c1 to cytochrome c. This article is part of a special issue entitled: Respiratory Complex III.

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Section: Reaction Between Cytochrome Bc1 and Cytochrome Cmentioning

confidence: 99%

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c

Millett

Havens

Rajagukguk

et al. 2013

Biochimica et Biophysica Acta (BBA) - Bioenergetics

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“…Region 1 has been identified as part of the cytochrome c-binding domain by carbodiimide modification studies (10,11), whereas region 2 has been implicated in cytochrome c binding by photoaffinity cross-linking studies (12). The amino terminus of subunit 8, consisting of eight consecutive glutamate residues, was also found to be important in binding cytochrome c in the carbodiimide modification studies (10,11). However, no electron density was observed for the N-terminal 14 residues of subunit 8, indicating that this segment is highly mobile.…”

Section: Definition Of the Cytochrome C-binding Domain By Kinetic Stumentioning

confidence: 99%

“…Extensive chemical modification studies have revealed that six or seven lysine amino groups surrounding the heme crevice of cytochrome c are involved in binding cytochrome bc 1 (6 -9). Studies utilizing a water-soluble carbodiimide have implicated the acidic residues 66, 67, 76, and 77 on bovine cytochrome c 1 in cytochrome c binding as well as acidic residues on the hinge protein (10,11). Acidic residues in sequence 165-174 have also been implicated in cytochrome c binding by photoaffinity cross-linking studies (12).…”

mentioning

confidence: 99%

Definition of the Interaction Domain for Cytochrome con the Cytochrome bc 1 Complex

Tian¹,

Sadoski²,

Zhang³

et al. 2000

Journal of Biological Chemistry

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“…The 17-kDa subunit is thought to be homologous to the hinge protein of the bovine-heart complex 111 [12,131. This hinge protein can be cross-linked to both cytochrome c1 [14,15] and cytochrome c [14]. The 37-kDa subunit is able to stabilize cytochrome c1 against breakdown by endogenous proteases in a cytochromeb-deficient enzyme and stimulates the association of cytochrome c1 with cytochrome c [14, 16, the 17-kDa subunit is entirely present outside the lipophilic core of the membrane facing the intermembrane space.…”

mentioning

confidence: 99%

Membrane topography of the subunits of ubiquinol – cytochrome‐c oxidoreductase of Saccharomyces cerevisiae

Hemrika

Berden

1990

European Journal of Biochemistry

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The topology of the subunits of ubiquinol–cytochrome‐c oxidoreductase of the yeast Saccharomyces cerevisiae has been determined using a digitonin/proteinase K assay. With this assay we were able selectively to disrupt the mitochondrial membranes and to identify the subunits which became proteinase‐K‐sensitive after disruption of either the outer or both outer and inner membranes. This approach confirmed previous indications for the localization of the core I protein, cytochrome c1, cytochrome b, the FeS protein and the 17‐kDa subunit, while it also provided direct evidence for the site of accessibility to proteinase K of the 14‐kDa and 11‐kDa subunits. The 14‐kDa subunit faces the mitochondrial matrix and the 11‐kDa subunit faces the intermembrane space.

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Interaction between cytochrome c and ubiquinone-cytochrome c oxidoreductase: A study with water-soluble carbodiimides

Cited by 23 publications

References 42 publications

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c

Design and use of photoactive ruthenium complexes to study electron transfer within cytochrome bc1 and from cytochrome bc1 to cytochrome c

Definition of the Interaction Domain for Cytochrome con the Cytochrome bc 1 Complex

Membrane topography of the subunits of ubiquinol – cytochrome‐c oxidoreductase of Saccharomyces cerevisiae

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