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Biogenesis of Cytochrome Oxidase and Cytochrome b in Neurospora crassa
1975In this article we would like to outline the close cooperation between the mitochondrial and cytoplasmic protein-synthesizing systems in mitochondrial biogenesis. The subject of our studies is two proteins of the mitochondrial membrane, cytochrome oxidase and cytochrome b.
Hanns Weiss +2 more
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1986
Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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Publisher Summary This chapter describes the purification of neutrophilic leukocytes from peripheral blood, the isolation of their membranes that are enriched in the cytochrome, the preparation of a solubilized oxidase, and the purification of the cytochrome itself.
Anthony W. Segal +3 more
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Assembly of Transmembrane b-Type Cytochromes and Cytochrome Complexes
2016Cytochromes are involved in charge-transfer reactions, and many cytochromes contain a transmembrane domain and are part of membrane-localized electron transfer chains. Protoporphyrin IX (heme b) is the first heme product in the tetrapyrrole/heme biosynthesis pathway.
Koch, Hans-Georg, Schneider, Dirk
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Genetics and biogenesis of cytochrome b.
Methods in enzymology, 1984We have reviewed here the genetic methods used for isolating and manipulating nuclear and mitochondrial mutants of bakers' yeast that affect the function and biogenesis of complex III of the mitochondrial respiratory chain. All the methods have been used with success in the past, and it is hoped that this compilation will aid biochemists in using these
P S, Perlman, H R, Mahler
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1955
Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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Publisher Summary Cytochrome b of mammalian tissue is a hemoprotein which in the reduced (ferrous) form has absorption bands centered at 564 mμ (α), 530 mμ (β), and 430 mμ (γ). In heart muscle extracts which contain both an active succinic dehydrogenase and cytochrome oxidase, the addition of succinate causes reduction of cytochrome b and aeration ...
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1975
Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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Publisher Summary Type b cytochromes are electron-carrying proteins, which contain protoheme IX as the prosthetic group. The position of α band of their absorption spectra in the ferrous state ranges from 554 to 566 nm. By the pyridine treatment they give the pyridine-protohemochrome with its α band at 556 nm.
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Isolation of cytochrome b form the cytochrome b/c1 complex of Rhodopseudomonas sphaeroides GA
1983The purification and the biochemical characterization of cytochrome b of the cytochrome b/c1 complex from Rhodobacter capsulatus is reported.
GABELLINI, NADIA, HAUSKA G.
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Proceedings of the National Academy of Sciences of the United States of America, 2022
Grace W Chong +2 more
exaly
Grace W Chong +2 more
exaly