Characterization of lysyl residues of NADH-cytochrome b5 reductase implicated in charge-pairing with active-site carboxyl residues of cytochrome b5 by site-directed mutagenesis of an expression vector for the flavoprotein.-Reference-Cited by-同舟云学术

Characterization of lysyl residues of NADH-cytochrome b5 reductase implicated in charge-pairing with active-site carboxyl residues of cytochrome b5 by site-directed mutagenesis of an expression vector for the flavoprotein.

Published:1992-02 Issue:4 Volume:267 Page:2519-2523
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Strittmatter P,Kittler J M,Coghill J E,Ozols J

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference32 articles.

1. A Form of Reduced Nicotinamide Adenine Dinucleotide-Cytochrome b5 Reductase Containing Both the Catalytic Site and an Additional Hydrophobic Membrane-binding Segment

2. A Function of Cytochrome b5 in Fatty Acid Desaturation by Rat Liver Microsomes

3. Purification and Properties of Rat Liver Microsomal Stearyl Coenzyme A Desaturase

4. Evidence for the participation of cytochrome b5 in hepatic microsomal mixed-function oxidation reactions

5. Involvement of cytochrome b5 in the oxidative desaturation of linoleic acid to γ-linolenic acid in rat liver microsomes

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