Results 31 to 40 of about 10,590 (289)

Loss of APD1 in Yeast Confers Hydroxyurea Sensitivity Suppressed by Yap1p Transcription Factor [PDF]

open access: yes, 2015
Ferredoxins are iron-sulfur proteins that play important roles in electron transport and redox homeostasis. Yeast Apd1p is a novel member of the family of thioredoxin-like ferredoxins.
Chan, LC   +8 more
core   +1 more source

Molecular Details on Multiple Cofactor Containing Redox Metalloproteins Revealed by Infrared and Resonance Raman Spectroscopies

open access: yesMolecules, 2021
Vibrational spectroscopy and in particular, resonance Raman (RR) spectroscopy, can provide molecular details on metalloproteins containing multiple cofactors, which are often challenging for other spectroscopies.
Célia M. Silveira   +6 more
doaj   +1 more source

Transcriptomic Responses of Four Pelagophytes to Nutrient (N, P) and Light Stress

open access: yesFrontiers in Marine Science, 2021
Pelagophytes are abundant picophytoplankton within open ocean ecosystems and the causative algae of harmful brown tide blooms in estuaries. The physiological capabilities facilitating the ecological success of pelagophytes in these diverse ecosystems ...
Yoonja Kang   +7 more
doaj   +1 more source

Pichia pastoris Fep1 is a [2Fe-2S] protein with a Zn finger that displays an unusual oxygen-dependent role in cluster binding [PDF]

open access: yes, 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
core   +4 more sources

The semiquinone swing in the bifurcating electron transferring flavoprotein/butyryl-CoA dehydrogenase complex from Clostridium difficile

open access: yesNature Communications, 2017
The electron-transferring flavoprotein / butyryl-CoA dehydrogenase (EtfAB/Bcd) complex catalyzes the reduction of crotonyl-CoA and ferredoxins by NADH in anaerobic microbes.
Julius K. Demmer   +4 more
doaj   +1 more source

Carbon Fixation in the Chemolithoautotrophic Bacterium Aquifex aeolicus Involves Two Low-Potential Ferredoxins as Partners of the PFOR and OGOR Enzymes

open access: yesLife, 2023
Aquifex aeolicus is a microaerophilic hydrogen- and sulfur -oxidizing bacterium that assimilates CO2 via the reverse tricarboxylic acid cycle (rTCA). Key enzymes of this pathway are pyruvate:ferredoxin oxidoreductase (PFOR) and 2-oxoglutarate:ferredoxin ...
Laura Prioretti   +9 more
doaj   +1 more source

Ferredoxin from Bacillus polymyxa

open access: yesBiochemical 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
openaire   +2 more sources

Ferredoxin—ferredoxin NADP reductase interaction [PDF]

open access: yesFEBS 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
openaire   +1 more source

Functional Analysis of an Appressorium-Specific Gene from Colletotrichum gloeosporioides

open access: yesHayati Journal of Biosciences, 2020
A novel gene (CAS2) specifically expressed during appressorium formation was isolated from Colletotrichum gloeosporioides using Differential Display RT-PCR.
Tri Puji Priyatno   +4 more
doaj   +1 more source

Distinct Physiological Roles of the Three Ferredoxins Encoded in the Hyperthermophilic Archaeon Thermococcus kodakarensis

open access: yesmBio, 2019
Control of electron flux is critical in both natural and bioengineered systems to maximize energy gains. Both small molecules and proteins shuttle high-energy, low-potential electrons liberated during catabolism through diverse metabolic landscapes ...
Brett W. Burkhart   +2 more
doaj   +1 more source

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