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2 edition of Studies of Wolinella succinogenes nitrite reductase. found in the catalog.

Studies of Wolinella succinogenes nitrite reductase.

Richard Blackmore

Studies of Wolinella succinogenes nitrite reductase.

by Richard Blackmore

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Published by University of East Anglia in Norwich .
Written in English


Edition Notes

Thesis (Ph.D), University of East Anglia, School of Biological Sciences, 1988.

ID Numbers
Open LibraryOL13924376M

In enzymology, a nitrite reductase (NO-forming) (EC ) is an enzyme that catalyzes the chemical reaction. nitric oxide + H 2 O + ferricytochrome c ⇌ nitrite + ferrocytochrome c + 2 H +. The 3 substrates of this enzyme are nitric oxide, H 2 O, and ferricytochrome c, whereas its 3 products are nitrite, ferrocytochrome c, and H +.. This enzyme belongs to the family of oxidoreductases. Higher plant nitrite reductase (NiR) is a monomeric chloroplastic protein catalysing the reduction of nitrite, the product of nitrate reduction, to ammonium. The expression of this enzyme is controlled at the transcriptional level by light and by the nitrogen source.

The reduction of nitrate to nitrite by nitrate reductase, and the reduction of nitrite to ammonium by nitrite reductase are two major procedures in the biological conversion of inorganic nitrate to ammonium, an eight-electron reduction process. NR has been proposed as an important enzymatic source of nitric oxide (NO). NR also plays a role in. cytochrome b5 reductase (66; EC ), whereas NR’s Cb is related to eu-karyotic cytochrome b5 (59), which is a redox partner of its reductase with both anchored in the endoplasmic reticulum, although soluble forms of these pro-teins also exist in mammalian systems (Figure 1b). The Mo-MPT and interface.

A nitrite reductase was identified and purified 11 ‐fold from the cytoplasmic fraction of Salmonella typhimurium grown anaerobically with nitrite as the sole nitrogen source. The enzyme required NADH as a cofactor and showed maximum in vitro reductase activity at pH Nitrite reductase is a dimeric molecule, composed of two chemically identical subunits. Each of the two polypetide chains is folded into two domains: the alpha helical c-type cytochrome domain (residues , the c domain), and a rigid beta propeller domain (residues , the d 1 - domain).


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Studies of Wolinella succinogenes nitrite reductase by Richard Blackmore Download PDF EPUB FB2

The sulfur reductase (EC ) is a constitutive enzyme in Desulfovibrio and Desulfomicrobium species, as it is also the case for the sulfur reductase from the sulfur-reducing eubacteria: W.

succinogenes DSMDSM Deutsche Sammlung von Mikroorganismen, Braunschweig, Germany. acetoxidans DSMand Sulfurospirillum (S.) deleyianum DSM. The six haem groups of the nitrite reductase enzyme isolated from Wolinella succinogenes are rapidly reduced by the addition of dithionite (S2O4(2-)).

The reduction, however, is not homogeneous. Two of the haem groups, namely those that show spectral characteristics typical of five-co-ordinated haem groups, are reduced in a dithionite Cited by: 7. Kinetic studies on the nitrite reductase of Wolinella succinogenes.

Blackmore R, Brittain T. The six haem groups of the nitrite reductase enzyme isolated from Wolinella succinogenes are rapidly reduced by the addition of dithionite (S2O4(2-)). The reduction, however, is not by: 7. Cytochrome c Nitrite Reductase from Wolinella succinogenes Cytochrome c nitrite reductase catalyzes the 6-electron reduction of nitrite to ammonia.

This second part of the respiratory pathway of nitrate ammonification is a key step in the biological nitrogen cycle. The x-ray Cited by: Purified nitrite reductase has a pH optimum in the range of and optimal activity at 57 degrees C.

Purified nitrite reductase also has hydroxylamine reductase activity, and the Km for. Abstract. The cytochrome nitrite reductase (ccNiR) from Desulfovibrio desulfuricans ATCC is able to reduce nitrite to ammonia in a six-electron transfer reaction.

Although extensively characterized from the spectroscopic and structural points-of-view, some of its kinetic aspects are still under explored. Assimilatory nitrate reductase is an enzyme of the assimilative metabolism involved in reduction of nitrate to nitrite is immediately reduced to ammonia (probably via hydroxylamine) by the activity of nitrite reductase.

The term assimilatory refers to the fact that the product of the enzymatic activity remains in the organism. Oliver Einsle, Petra Stach, Albrecht Messerschmidt, Jörg Simon, Achim Kröger, Robert Huber, Peter M. Kroneck. Abstract. The genus Wolinella was proposed (as was the genus Campylobacter) for certain species originally classified in the genus Vibrio and was placed in the family Bacteroidaceae (Krieg and Holt, ).Wolinella was named for Dr.

Meyer Wolin, an American bacteriologist who first described a microorganism (Vibrio succinogenes) with a metabolism that characterizes this genus. In denitrification, the nitrite reductase is either a cytochrome cd 1, or a copper protein [3,4].

During nitrate-ammonification nitrate is reduced to nitrite as the only liberated intermediate that is subsequently converted to ammonia in a six-electron step by a cytochrome c nitrite reductase [4]. Cytochrome c nitrite reductases from Wolinella succinogenes wild-type, KH- QE- YF- and StopI-variant were purified to homogenity both from the soluble and the membrane fraction.

Reduction kinetics of resting and redox-cycled forms of the nitrite reductase from the anaerobic rumen bacterium Wolinella succinogenes were studied by stopped-flow reaction techniques. Single-turnover reduction of the enzyme by dithionite occurred in 2 kinetic phases for both forms of enzyme.

When the resting form of the enzyme was subjected to a single-turnover reduction by dithionite, the. Nitrite reductase (EC ) has been purified fold from spinach leaves. The enzyme catalyzes the reduction of nitrite to ammonia, with the use of reduced form of methyl viologen and ferredoxin.

A stoichiometry of one molecule of nitrite reduced per molecule of ammonia formed has been found. The nitrate and nitrite reduction test determines the ability of bacteria to produce the enzyme nitrate reductase and reduce nitrate and/or nitrite.

The nitrate and nitrite test is useful for the identification of bacteria and separating members of the family Enterobacteriaceae from other gram-negative bacilli.

The nitrite anion is reduced to nitric oxide (NO•) as oxygen tension decreases. Whereas this pathway modulates hypoxic NO• signaling and mitochondrial respiration and limits myocardial infarction in mammalian species, the pathways to nitrite bioactivation remain uncertain.

Studies suggest that hemoglobin and myoglobin may subserve a fundamental physiological function as hypoxia. (2) nitrite reductase: NO 2 − + 6 ferredoxin reduced + 8 H + → NH 4 + + 6 ferredoxin oxidized + 2 H 2 O Nitrate reductase (NR), 1 1 The abbreviation used is: NR, nitrate reductase.

the rate‐limiting enzyme, is a cytoplasmic enzyme usually found in both roots and shoots [ 4 ]. Nitrate reductase (NAD[P]H) is expressed in variety of organisms including bacteria, fungi, algae, and higher plants which have capacity to use nitrate as their sole source of mental studies show that nitrate reductase (NAD[P]H) is ,Daltons.

Packaging. A protein with molecular mass of 67 kilodaltons is immunoprecipitated from in vitro translated products obtained from rabbit reticulocyte lysate primed with polyadenylated RNA from nitrate treated illuminated pea seedlings. This protein resembles the native nitrite reductase because of its competitive elimination when immunoprecipitation of in vitro translated products was carried out in the.

Previous studies have demonstrated that nitrite is an endocrine store of NO that may play an important role in hypoxic vasodilation. Nitrite can be converted to NO enzymatically by deoxyhemoglobin, in a reaction that is under allosteric control with a maximum reaction rate near the hemoglobin P In this study, we characterize the nitrite reductase activity of deoxymyoglobin.

Transgenic plants of Arabidopsis bearing the spinach (Spinacia oleracea) nitrite reductase (NiR, EC [][1]) gene that catalyzes the six-electron reduction of nitrite to ammonium in the second step of the nitrate assimilation pathway were produced by use of the cauliflower mosaic virus 35S promoter and nopaline synthase terminator.

Integration of the gene was confirmed by a genomic. Nitrate reduction to ammonia via nitrite occurs widely as an anabolic process through which bacteria, archaea, and plants can assimilate nitrate into cellular biomass.

Escherichia coli and related enteric bacteria can couple the eight-electron reduction of nitrate to ammonium to growth by coupling the nitrate and nitrite reductases involved to energy-conserving respiratory electron transport.Nitrate reductase (NR) is regulated at the transcriptional and translational levels induced by light, nitrate, and possibly a negative feedback mechanism.

First, nitrate assimilation is initiated by the uptake of nitrate from the root system, reduced to nitrite by nitrate reductase, and then nitrite is reduced to ammonia by nitrite reductase.A NapC/NirT-type cytochrome c (NrfH) is the mediator between the quinone pool and the cytochrome c nitrite reductase of Wolinella succinogenes.

Mol. Microbiol. (). Simon J, Sanger M, Schuster SC, Gross R. Electron transport to periplasmic nitrate reductase (NapA) of Wolinella succinogenes is independent of a NapC protein. Mol.