Affordable Access

Circular dichroism spectra of NADH-cytochrome b5 reductase purified from rabbit erythrocytes.

Authors
  • Yubisui, T
  • Takeshita, M
Type
Published Article
Journal
Biochemistry international
Publication Date
Feb 01, 1984
Volume
8
Issue
2
Pages
319–327
Identifiers
PMID: 6477604
Source
Medline
License
Unknown

Abstract

Soluble oxidized NADH-cytochrome b5 reductase from rabbit erythrocytes showed characteristic negative CD bands at 285 and 460-490 nm and positive CD bands at 310 and 370-390 nm. By the anaerobic reduction of the enzyme with NADH, the sign of the CD spectrum was reversed. The CD spectrum of the NADPH-reduced enzyme was different from that of the NADH-reduced one and was closely similar to that of the dithionite-reduced one. Modifications of cysteine or tyrosine residues in the enzyme were shown to cause no release of flavin or to weaken the binding of flavin, as compared to the immediate release of flavin with HC1 or NaOH.

Report this publication

Statistics

Seen <100 times