1983
DOI: 10.1016/0006-291x(83)90411-4
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Interaction between cytochrome c and ubiquinone-cytochrome c oxidoreductase: A study with water-soluble carbodiimides

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Cited by 23 publications
(11 citation statements)
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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%
“…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%
“…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%
“…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%