Title : Molecular modeling studies of the DCCD-treated cytochrome bc1 complex: predicted conformational changes and inhibition of proton translocation.

Pub. Date : 2002 Apr

PMID : 12018891






3 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 Dicyclohexylcarbodiimide (DCCD) binds covalently to an acidic amino acid located in the cd loop connecting membrane-spanning helices C and D of cytochrome b resulting in an inhibition of proton translocation in the cytochrome bc1 complex with minimal effects on the steady state rate of electron transfer. Dicyclohexylcarbodiimide cytochrome b Saccharomyces cerevisiae S288C
2 Dicyclohexylcarbodiimide (DCCD) binds covalently to an acidic amino acid located in the cd loop connecting membrane-spanning helices C and D of cytochrome b resulting in an inhibition of proton translocation in the cytochrome bc1 complex with minimal effects on the steady state rate of electron transfer. Dicyclohexylcarbodiimide cytochrome b Saccharomyces cerevisiae S288C
3 Single turnover studies performed with the yeast cytochrome bc1 complex indicated that the initial phase of cytochrome b reduction was inhibited 25-45% in the DCCD-treated cytochrome bc1 complex, while the rate of cytochrome c1 reduction was unaffected. Dicyclohexylcarbodiimide cytochrome b Saccharomyces cerevisiae S288C