Immunochemical studies on electron transport chains involving cytochrome P-450. The role of the iron-sulfur protein, adrenodoxin, in mixed-function oxidation reactions

1972 ◽  
Vol 150 (1) ◽  
pp. 105-115 ◽  
Author(s):  
Jeffrey Baron ◽  
Wayne E. Taylor ◽  
Bettie Sue Siler Masters
Keyword(s):  
Electron Transport ◽  
Oxidation Reactions ◽  
Iron Sulfur ◽  
Electron Transport Chains ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Cytochrome P 450

scholarly journals A Model of Aerobic and Anaerobic Metabolism of Hydrogen in the Extremophile Acidithiobacillus ferrooxidans

2020 ◽  
Vol 11 ◽  
Author(s):  
Jiri Kucera ◽  
Jan Lochman ◽  
Pavel Bouchal ◽  
Eva Pakostova ◽  
Kamil Mikulasek ◽  
...  
Keyword(s):  
Acidithiobacillus Ferrooxidans ◽  
Hydrogen Oxidation ◽  
Current Knowledge ◽  
Proton Efflux ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Terrestrial Subsurface ◽  
Aerobic And Anaerobic

Hydrogen can serve as an electron donor for chemolithotrophic acidophiles, especially in the deep terrestrial subsurface and geothermal ecosystems. Nevertheless, the current knowledge of hydrogen utilization by mesophilic acidophiles is minimal. A multi-omics analysis was applied on Acidithiobacillus ferrooxidans growing on hydrogen, and a respiratory model was proposed. In the model, [NiFe] hydrogenases oxidize hydrogen to two protons and two electrons. The electrons are used to reduce membrane-soluble ubiquinone to ubiquinol. Genetically associated iron-sulfur proteins mediate electron relay from the hydrogenases to the ubiquinone pool. Under aerobic conditions, reduced ubiquinol transfers electrons to either cytochrome aa3 oxidase via cytochrome bc1 complex and cytochrome c4 or the alternate directly to cytochrome bd oxidase, resulting in proton efflux and reduction of oxygen. Under anaerobic conditions, reduced ubiquinol transfers electrons to outer membrane cytochrome c (ferrireductase) via cytochrome bc1 complex and a cascade of electron transporters (cytochrome c4, cytochrome c552, rusticyanin, and high potential iron-sulfur protein), resulting in proton efflux and reduction of ferric iron. The proton gradient generated by hydrogen oxidation maintains the membrane potential and allows the generation of ATP and NADH. These results further clarify the role of extremophiles in biogeochemical processes and their impact on the composition of the deep terrestrial subsurface.

scholarly journals Immunofluorescent localization of 25-hydroxyvitamin-D3-1 alpha-hydroxylase ferredoxin in the renal tissue of chick.

1979 ◽  
Vol 27 (6) ◽  
pp. 1041-1045 ◽  
Author(s):  
J G Ghazarian ◽  
J C Garancis
Keyword(s):  
Vitamin D3 ◽  
Renal Tissue ◽  
Mitochondrial Localization ◽  
Immunofluorescent Localization ◽  
Iron Sulfur ◽  
Immunofluorescence Studies ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Cytochrome P 450 ◽  
Convoluted Tubules

The chick renal mitochondrial 25-hydroxyvitamin-D3-1 alpha-hydroxylase is composed of three proteins, namely, cytochrome P-450, iron-sulfur protein (ferredoxin) and flavoprotein. Antibodies were raised in rabbits against homogeneous preparations of the ferredoxin. The antibodies were used in indirect immunofluorescence studies to localize the ferrdoxin along the nephron of renal tissues obtained either from vitamin D3-deficient or vitamin D3-sufficient chicks. The ferredoxin is predominantly localized in the glomerulus and proximal convoluted tubules. These results suggest that, in addition to the mitochondrial localization of the 1-hydroxylase, the enzyme may also be present in renal nuclei. The amount of the ferredoxin in kidney, as evidenced by the intensity of fluorescence, appeared to be independent of the vitamin D status of the chick. This finding indicated that changes in the concentration of the renal ferredoxin is not a major factor in the regulation of the 1-hydroxylase activity.

TESTICULAR CYTOCHROME P-450 AND IRON-SULFUR PROTEIN AS RELATED TO STEROID METABOLISM

1973 ◽  
Vol 212 (1 Multienzyme S) ◽  
pp. 406-419 ◽  
Author(s):  
J. Ian Mason ◽  
Ronald W. Estabrook ◽  
John L. Purvis
Keyword(s):  
Steroid Metabolism ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Cytochrome P 450

Ischemic Injury to Mitochondrial Electron Transport in the Aging Heart: Damage to the Iron–Sulfur Protein Subunit of Electron Transport Complex III

2001 ◽  
Vol 385 (1) ◽  
pp. 117-128 ◽  
Author(s):  
Edward J. Lesnefsky ◽  
Tatyana I. Gudz ◽  
Catharina T. Migita ◽  
Masao Ikeda-Saito ◽  
Medhat O. Hassan ◽  
...  
Keyword(s):  
Electron Transport ◽  
Ischemic Injury ◽  
Complex Iii ◽  
Protein Subunit ◽  
Aging Heart ◽  
Heart Damage ◽  
Iron Sulfur ◽  
Sulfur Protein ◽  
Iron Sulfur Protein ◽  
Transport Complex
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