Measurement of the oxidation‐reduction potentials of amicyanin and c‐type cytochromes from Paracoccus denitrificans

FEBS Letters

Knaff, David B.¹  Gray, Kevin A.¹  Husain, Mazhar²  Davidson, Victor L.² 

[1] Department of Chemistry and Biochemistry, Texas Tech University, Lubbock, TX 74909 USA;Molecular Biology Division, Veterans Administration Medical Center, San Francisco, CA 94121, USA, Department of Biochemistry and Biophysics, University of California, San Francisco, CA 94143, USA

关键词: Amicyanin;    Cytochrome c;    Methylamine dehydrogenase;    Methylotrophic bacteria;    Redox potential;    (Paracoccus denitrificans);    E m;    midpoint potential;    MADH;    methylamine dehydrogenase;   

DOI  :  10.1016/0014-5793(86)81496-X

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

The oxidation-reduction potentials of four periplasmic electron carrier proteins from Paracoccus denitrificans have been determined. Their midpoint potentials are: amicyanin, 294±6 mV; cytochrome c-550, 253±5 mV; cytochrome c-551i, 190±4 mV, and cytochrome c-553i, 148±5 mV. Although rapid amicyanin-mediated transfer of electrons from methylamine dehydrogenase to cytochrome c-551i was observed, reduced amicyanin did not reduce oxidized cytochrome c-551i in the absence of methylamine dehydrogenase.

【 授权许可】

Unknown