Results 1 to 10 of about 3,338 (186)
Low-energy spectrum of iron-sulfur clusters directly from many-particle quantum mechanics [PDF]
, 2014 FeS clusters are a universal biological motif. They carry out electron transfer, redox chemistry, and even oxygen sensing, in diverse processes including nitrogen fixation, respiration, and photosynthesis. The low-lying electronic states are key to their
Chan, Garnet Kin-Lic +3 more
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Ferredoxin from Bacillus polymyxa
Biochemical and Biophysical Research Communications, 1971 A ferredoxin has been purified from Bacillus polymyxa, strain Hino, a facultative N2-fixing organism. Optical and electron spin resonance spectra of the ferredoxin have been recorded, and its molecular weight is approximately 9,000. The ferredoxin is reduced reversibly by H2 in the presence of hydrogenase from Clostridium pasteurianum or B.
Y I, Shethna +2 more
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Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding [PDF]
, 2016 Fep1, the iron-responsive GATA factor from the methylotrophic yeast Pichia pastoris, has been characterised both in vivo and in vitro. This protein has two Cys(2)-Cys(2) type zinc fingers and a set of four conserved cysteines arranged in a Cys-X-5-Cys-X ...
Battistoni, Andrea +8 more
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Ferredoxin—ferredoxin NADP reductase interaction [PDF]
FEBS Letters, 1984 Ferredoxin‐NADP reductase (FNR) and ferredoxin form a complex when the former is membrane‐bound as they do when both components are in solution, with the same dissociation constant. The rate constant of NADP photoreduction, first order with respect to the complex, is more than 20‐times higher when FNR is membrane‐bound than when the enzyme is in ...
Forti, Giorgio, Bracale, Marcella
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Mitochondrial ferredoxin determines vulnerability of cells to copper excess [PDF]
, 2017 The essential micronutrient copper is tightly regulated in organisms, as environmental exposure or homeostasis defects can cause toxicity and neurodegenerative disease.
Avery, Simon V. +2 more
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Ferredoxin binding site on ferredoxin: NADP+ reductase [PDF]
European Journal of Biochemistry, 1993 The chloroplast enzyme ferredoxin:NADP+ reductase (FNR) catalyzes the reduction of NADP+ by ferredoxin (Fd). FNR and Fd form a 1:1 complex that is stabilized by electrostatic interactions between acidic residues of Fd and basic residues of FNR. To localize lysine residues at the Fd binding site of FNR, the FNR:Fd complex (both proteins from spinach ...
I, Jelesarov +5 more
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Identification of ferredoxin II as a major calcium binding protein in the nitrogen-fixing symbiotic bacterium Mesorhizobium loti [PDF]
, 2015 BACKGROUND: Legumes establish with rhizobial bacteria a nitrogen-fixing symbiosis which is of the utmost importance for both plant nutrition and a sustainable agriculture.
Damiani, Ernesto +6 more
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A synthetic system links FeFe-hydrogenases to essential E. coli sulfur metabolism [PDF]
, 2011 Background FeFe-hydrogenases are the most active class of H2-producing enzymes known in nature and may have important applications in clean H2 energy production.
Buz Barstow +5 more
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, 1994 This book covers material that could be included in a one-quarter or one-semester course in bioinorganic chemistry for graduate students and advanced undergraduate students in chemistry or biochemistry.
Bertini, Ivano +3 more
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Adrenodoxin—A versatile ferredoxin [PDF]
IUBMB Life, 2012 AbstractMammalian adrenodoxin (Adx) has been known for many years as an essential electron mediator in mitochondrial cytochrome P450 systems. Because of its ability to support several cytochrome P450 enzymes, it is involved not only in adrenal steroid hormone biosynthesis but also in vitamin D and bile acid metabolism.
Kerstin Maria, Ewen +2 more
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