Pyridoxal phosphate modified cytochromes c. Identification and electron transfer properties-Reference-Cited by-同舟云学术

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Pyridoxal phosphate modified cytochromes c. Identification and electron transfer properties

Published:1984-06 Issue:3 Volume:765 Page:329-339
ISSN:0005-2728
Container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics
language:en
Short-container-title:Biochimica et Biophysica Acta (BBA) - Bioenergetics

Author:

Atanasov Boris P.,Mitovska Maria I.,Mancheva Ivanka N.,Kossekova Ganka P.,Tchorbanov Bojidar P.,Christova Petia,Dancheva Kirana I.

Publisher

Elsevier BV

Subject

Cell Biology,Biochemistry,Biophysics

Reference31 articles.

1. Definition of cytochrome c binding domains by chemical modification. I. Reaction with 4-chloro-3,5-dinitrobenzoate and chromatographic separation of singly substituted derivatives.

2. Definition of cytochrome c binding domains by chemical modification. II. Identification and properties of singly substituted carboxydinitrophenyl cytochromes c at lysines 8, 13, 22, 27, 39, 60, 72, 87, and 99.

3. Distinction between oxidizing and reducing sites of cytochromeCby chemical modification with pyridoxal phosphate

4. Use of specific trifluoroacetylation of lysine residues in cytochrome c to study the reaction with cytochrome b5, cytochrome c1, and cytochrome oxidase

5. Definition of enzymic interaction domains on cytochrome c. Purification and activity of singly substituted carboxydinitrophenyl-lysine 7, 25, 73, 86, and 99 cytochromes c.

Cited by 11 articles. 订阅此论文施引文献订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献

1. An Essential Lysyl Residue (Lys208) in the Substrate-Binding Site of Porcine FAD-Containing Monooxygenase;European Journal of Biochemistry;2008-06-28

2. Local electrostatic potentials in pyridoxal phosphate labelled horse heart cytochrome c;Journal of Photochemistry and Photobiology B: Biology;1997-01

3. Characterization of pyridoxal phosphate as an optical label for measuring electrostatic potentials in proteins;Journal of Photochemistry and Photobiology B: Biology;1996-01

4. An Essential Lysyl Residue (Lys208) in the Substrate-Binding Site of Porcine FAD-Containing Monooxygenase;European Journal of Biochemistry;1995-05

5. Identification of essential lysyl and cysteinyl residues, and the amino acid sequence at the substrate-binding site of retinal oxidase;Biochimica et Biophysica Acta (BBA) - General Subjects;1995-04

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