Results 71 to 80 of about 215,309 (173)

The genome of Pelobacter carbinolicus reveals surprising metabolic capabilities and physiological features [PDF]

, 2012
Background The bacterium Pelobacter carbinolicus is able to grow by fermentation, syntrophic hydrogen/formate transfer, or electron transfer to sulfur from short-chain alcohols, hydrogen or formate; it does not oxidize acetate and is not known to ferment
Cliff S Han, Derek R Lovley, Miriam L Land, Muktak Aklujkar, Olga Chertkov, Peter Brown, Raymond DiDonato, Shelley A Haveman   +7 more
core   +2 more sources

CyanoNews (Vol. 11, No. 1, February 1995) [PDF]

, 1995
CyanoNews was a newsletter that served the cyanobacteriological community from 1985 to 2003, with content provided by readers (sort of a blog before there were blogs). The newsletter reported new findings from the lab, summaries of recent meetings (often
Elhai, Jeff
core   +1 more source

A General Tool for Engineering the NAD/NADP Cofactor Preference of Oxidoreductases [PDF]

, 2017
The ability to control enzymatic nicotinamide cofactor utilization is critical for engineering efficient metabolic pathways. However, the complex interactions that determine cofactor-binding preference render this engineering particularly challenging ...
Arnold, Frances H., Baumschlager, Armin, Brinkmann-Chen, Sabine, Cahn, Jackson K. B., Mayo, Stephen L., Werlang, Caroline A.   +5 more
core   +2 more sources

Association of ferredoxin-NADP+ reductase with NADP(H) specificity and oxidation-reduction properties.

Journal of Biological Chemistry, 1986
The equilibrium properties of the NADP+ binding site of ferredoxin-NADP+ reductase (FNR, or Fd-NADP+ reductase) were examined with regard to specificity in binding, and with regard to the oxidation-reduction properties of the FNR.NADP+ complex.
C. Batie, H. Kamin
semanticscholar   +1 more source

Comparison of the Electrostatic Binding Sites on the Surface of Ferredoxin for Two Ferredoxin-dependent Enzymes, Ferredoxin-NADP+ Reductase and Sulfite Reductase*

Journal of Biological Chemistry, 1999
Plant-type ferredoxin (Fd), a [2Fe-2S] iron-sulfur protein, functions as an one-electron donor to Fd-NADP+ reductase (FNR) or sulfite reductase (SiR), interacting electrostatically with them. In order to understand the protein-protein interaction between
Tetsuyuki Akashi, T. Matsumura, T. Ideguchi, K. Iwakiri, Takenobu Kawakatsu, I. Taniguchi, T. Hase   +6 more
semanticscholar   +1 more source

Competition between C-terminal Tyrosine and Nicotinamide Modulates Pyridine Nucleotide Affinity and Specificity in Plant Ferredoxin-NADP+ Reductase*

Journal of Biological Chemistry, 2000
Chloroplast ferredoxin-NADP+reductase has a 32,000-fold preference for NADPH over NADH, consistent with its main physiological role of NADP+ photoreduction for de novo carbohydrate biosynthesis. Although it is distant from the 2′-phosphoryl group of NADP+
L. Piubelli, A. Aliverti, A. Arakaki, N. Carrillo, E. Ceccarelli, P. Karplus, G. Zanetti   +6 more
semanticscholar   +1 more source

Thioredoxin and evolution [PDF]

Comparisons of primary structure have revealed significant homology between the m type thioredoxins of chloroplasts and the thioredoxins from a variety of bacteria.
Buchanan, B. B.
core   +1 more source

Blue-fluorescence of NADPH as an indicator of marine primary production [PDF]

, 2004
Nicotinamide Adenine Dinucleotide Phosphate (NADPH) is the primary product of photosynthesisand can therefore serve as an indicator of biomass and photosynthetic activity.
Grossart, H-P., Reuter, R., Steigenberger, S., Terjung, F.   +3 more
core  

Die Funktion des Responseregulators ARR2 in der Entwicklung von Arabidopsis thaliana [PDF]

, 2004
In dieser Arbeit konnte mittels physiologischer Experimente, Expressionsanalysen, Phosphorylierungsassays und Transaktivierungsanalysen eine komplexe Funktion von ARR2 in verschiedenen Signaltransduktionswegen von Arabidopsis aufgedeckt werden.
Haß, Claudia
core  

Polarized time-resolved fluorescence of C-phycocyanin from Mastigocladus laminosus [PDF]

, 1984
Hefferle, P., John, Wolfhart, Scheer, Hugo, Schneider, Siegfried, Sybesma, C.   +4 more
core   +1 more source