Results 221 to 230 of about 358,220 (258)
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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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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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Extracellular cytochrome nanowires appear to be ubiquitous in prokaryotes
Cell, 2023Christopher Rensing +2 more
exaly
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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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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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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