نتایج جستجو برای: nitrogenase

تعداد نتایج: 2309  

Journal: :The Journal of biological chemistry 2006
Jiro Nomata Tadashi Mizoguchi Hitoshi Tamiaki Yuichi Fujita

In most photosynthetic organisms, the chlorin ring structure of chlorophyll a is formed by the reduction of the porphyrin D-ring by the dark-operative nitrogenase-like enzyme, protochlorophyllide reductase (DPOR). Subsequently, the chlorin B-ring is reduced in bacteriochlorophyll biosynthesis to form a bacteriochlorin ring structure. Phenotypic analysis of mutants lacking one of three genes, bc...

Journal: :Proceedings of the National Academy of Sciences of the United States of America 1978
F O'gara K T Shanmugam

Mutant strains of Rhizobium trifolii that induce nitrogenase activity in the free-living state were isolated. These strains, unlike the wild type, nodulated soybean and mungbean plants, producing effective nodules. One of the strains, strain DT72, also nodulated clover but the nodules were ineffective. Strain DT125 consumed hydrogen gas from the gas phase, which can be coupled to nitrogenase ac...

Journal: :ACS Catalysis 2021

The Haber–Bosch process conventionally reduces N2 to ammonia at 200 bar and 500 °C. Under ambient conditions, i.e., room temperature pressure, can be converted into by the nitrogenase molecule lithium-containing solid electrodes in nonaqueous media. In this work, we explore catalyst space for reduction reaction under conditions. We describe on basis of *N2 binding energy versus *H energy; find ...

Journal: :Biochemistry 1998
W N Lanzilotta V D Parker L C Seefeldt

Nitrogenase-catalyzed substrate reduction reactions require electron transfer between two component proteins, the iron (Fe) protein and the molybdenum-iron (MoFe) protein, in a reaction that is coupled to the hydrolysis of MgATP. In the present work, electron transfer (Marcus) theory has been applied to nitrogenase electron transfer reactions to gain insights into possible roles for MgATP in th...

Journal: :Biochemical Society transactions 1996
L J Dougherty E G Brown J R Gallon

Gloeothece is a non-heterocystous, unicellular cyanobacterium that is capable of aerobic N, fixation [I]. As in other diazotrophs, nitrogenase in Gloeothece consists of a MoFe-protein and an Feprotein. The Faprotein of Gloeothece nitrogenase can be resolved into two different, though antigenically similar, forms by SDSPAGE. These two forms have apparent M, values of 38 500 and 40 000 respective...

Journal: :Plant physiology 1975
T M Ching S Hedtke S A Russell H J Evans

Dark treatment of 25-day-old greenhouse-grown plants of inoculated soybean (Glycine max var. Chippewa) for 1 day reduced ATP by 70%, sucrose by 60%, total adenosine phosphates by 60%, ATP/ADP ratio by 55%, nitrogenase activity by 50%, and energy charge by 15% in nodules. The close correlation between nitrogenase activity and these energy parameters indicates that they may play a major role in r...

Journal: :Journal of bacteriology 1985
J E Schultz J W Gotto P F Weaver D C Yoch

Rhodospirillum rubrum was shown to grow fermentatively on fructose with N2 as a nitrogen source. The nitrogenase activity of these cells was regulated by the NH4+ switch-off/switch-on mechanism in a manner identical to that for photosynthetically grown cells. In vitro, the inactive nitrogenase Fe protein from fermenting cells was reactivated by an endogenous membrane-bound, Mn2+-dependent activ...

Journal: :The Biochemical journal 1993
M J Dilworth M E Eldridge R R Eady

During the reduction of N2 by V-nitrogenase at 30 degrees C, some hydrazine (N2H4) is formed as a product in addition to NH3 [Dilworth and Eady (1991) Biochem. J. 277, 465-468]. We show here the following. (1) That over the temperature range 30-45 degrees C the apparent Km for the reduction of N2 to yield these products is the same, but increases from 30 to 58 kPa of N2. On increasing the tempe...

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