Structure Analysis and Comparative Characterization of the Cytochrome c′ and Flavocytochrome c from Thermophilic Purple Photosynthetic Bacterium Thermochromatium tepidum

Biochemistry ◽  
2012 ◽  
Vol 51 (33) ◽  
pp. 6556-6567 ◽  
Author(s):  
Yu Hirano ◽  
Yukihiro Kimura ◽  
Hideaki Suzuki ◽  
Kunio Miki ◽  
Zheng-Yu Wang
Keyword(s):  
Cytochrome C ◽  
Structure Analysis ◽  
Photosynthetic Bacterium ◽  
Comparative Characterization ◽  
Purple Photosynthetic Bacterium ◽  
Flavocytochrome C

Structure analysis and characterization of the cytochrome c-554 from thermophilic green sulfur photosynthetic bacterium Chlorobaculum tepidum

2013 ◽  
Vol 118 (3) ◽  
pp. 249-258 ◽  
Author(s):  
Long-Jiang Yu ◽  
Masaki Unno ◽  
Yukihiro Kimura ◽  
Kasumi Yanagimoto ◽  
Hirozo Oh-oka ◽  
...  
Keyword(s):  
Cytochrome C ◽  
Structure Analysis ◽  
Photosynthetic Bacterium ◽  
Chlorobaculum Tepidum ◽  
Green Sulfur

Characterization of Two Soluble Basic Cytochromes Isolated from the Anoxygenic Phototrophic Sulfur Bacterium Chlorobium phaeobacteroides

1989 ◽  
Vol 44 (1-2) ◽  
pp. 71-76 ◽  
Author(s):  
Ulrich Fischer
Keyword(s):  
Molecular Weight ◽  
Cytochrome C ◽  
Redox Potential ◽  
Isoelectric Point ◽  
Gel Filtration ◽  
Exchange Chromatography ◽  
Chlorobium Phaeobacteroides ◽  
Flavocytochrome C ◽  
Reduced State

Abstract Chlorobium phaeobacteroides contains two soluble basic c-type cytochromes, a flavocytochrome c-552 and a small cytochrome c-555. Both electron transfer proteins were highly purified by ion exchange chromatography and gel filtration. The flavocytochrome c-552 exhibits maxima at 552 nm, 523 nm and 416 nm in the reduced state and at 409.5 nm with two shoulders at 440 nm and 480 nm in the oxidized form. The best purity index (A280/A416)obtained was 0.65. The molecular properties of this flavocytochrome are as follows: isoelectric point, pH 9.5 - 10; redox potential, +63 mV; molecular weight, 56,000. Cytochrome c-555 is a small basic hemoprotein with an isoelectric point of pH 9.5 - 10, a molecular weight of 9,500 and a midpoint redox potential of +105 mV. The best purity index {A280/A418) obtained was 0.176. The oxidized form of this cytochrome has a maximum at 411.5 nm, while the reduced state shows three maxima (α-band at 554.5 nm; β-band at 523 nm, and γ-band at 418 nm). The a-band is asymmetrical with a typical shoulder at 551 nm.

scholarly journals The purification and characterization of 4-ethylphenol methylenehydroxylase, a flavocytochrome from Pseudomonas putida JD1

1989 ◽  
Vol 263 (2) ◽  
pp. 431-437 ◽  
Author(s):  
C D Reeve ◽  
M A Carver ◽  
D J Hopper
Keyword(s):  
Cytochrome C ◽  
Redox Potential ◽  
Pseudomonas Putida ◽  
Gel Filtration ◽  
Purification And Characterization ◽  
Alkyl Groups ◽  
Flavocytochrome C

The enzyme 4-ethylphenol methylenehydroxylase was purified from Pseudomonas putida JD1 grown on 4-ethylphenol. It is a flavocytochrome c for which the Mr was found to be 120,000 by ultracentrifuging and 126,000 by gel filtration. The enzyme consists of two flavoprotein subunits each of Mr 50,000 and two cytochrome c subunits each of Mr 10,000. The redox potential of the cytochrome is 240 mV. Hydroxylation proceeds by dehydrogenation and hydration to give 1-(4′-hydroxyphenyl)ethanol, which is also dehydrogenated by the same enzyme to 4-hydroxyacetophenone. The enzyme will hydroxylate p-cresol but is more active with alkylphenols with longer-chain alkyl groups. It is located in the periplasm of the bacterium.

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