Unknown

Dataset Information

0

Reactions of cytochrome c oxidase with sodium dithionite.


ABSTRACT: The reduction of cytochrome c oxidase (EC 1.9.3.1) by dithionite was investigated by stopped-flow spectrophotometry and flow-flash techniques in the presence of CO. Of the two haem groups present in the enzyme, that associated with cytochrome alpha is the first reduced. The second-order rate constants for reduction of a number of redox proteins (cytochrome c, stellacyanin and azurin) by the S2O4(2-) and SO2.- anions are reported, and the values are compared with those determined for cytochrome c oxidase. These results are discussed in terms of the accessibility and charge distribution of the electron-entry site of cytochrome c oxidase.

SUBMITTER: Jones GD 

PROVIDER: S-EPMC1154069 | biostudies-other | 1983 Jan

REPOSITORIES: biostudies-other

Similar Datasets

2020-10-07 | GSE159080 | GEO
| S-EPMC6036987 | biostudies-literature
| S-EPMC166378 | biostudies-literature
| S-EPMC8569811 | biostudies-literature
| S-EPMC1163900 | biostudies-other
| S-EPMC1186060 | biostudies-other
| S-EPMC4220735 | biostudies-literature
| S-EPMC1166276 | biostudies-other
| S-EPMC1153594 | biostudies-other
| S-EPMC4948581 | biostudies-literature