Zobrazeno 1 - 10
of 201
pro vyhledávání: '"R, Timkovich"'
Publikováno v:
Biochemistry. 34:5248-5251
While isolating siroheme from enzymes or whole cells of Desulfovibrio species, it was discovered that the main product after metal removal and esterification was not the octamethyl ester derivative of sirohydrochlorin, but a monoamide, heptamethyl es
Publikováno v:
Bioorganic Chemistry. 22:284-293
Rubredoxin-oxygen oxidoreductase (ROO) from the sulfate-reducing bacterium Desulfovibrio gigas, is an unusual terminal oxidase capable of reducing molecular O2 to water. The nature of its heme prosthetic groups has been investigated. It was found to
Publikováno v:
Journal of Biological Chemistry. 265:13498-13500
The biosynthetic origin of methyl groups in heme d1 isolated from the nitrite reductase cytochrome cd1 was investigated by a stable isotope labeling experiment. Pseudomonas aeruginosa (American Type Culture Collection strain 19429) was grown on a min
Publikováno v:
European journal of biochemistry. 232(3)
The genetic organization of the nirD locus of Pseudomonas stutzeri ZoBell, necessary for a catalytically active cytochrome cd1 (EC 1.9.3.2), was determined. The locus comprises the unidirectionally transcribed open reading frames nirFDLGH, downstream
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Autor:
A N, Qabar, M S, Stern, D A, Walz, J T, Chiu, R, Timkovich, J S, Wall, O H, Kapp, S N, Vinogradov
Publikováno v:
Journal of molecular biology. 222(4)
The molecular dimensions of the extracellular, hexagonal bilayer chlorocruorin of the polychaete Eudistylia vancouverii, determined by scanning transmission electron microscopy (STEM) of negatively stained specimens, were diameter of 27.5 nm and heig
Autor:
R, Timkovich
Publikováno v:
Biochemistry. 29(33)
15N-1H correlation spectroscopy with detection at the 1H frequency has been used at natural abundance to detect nitrogen nuclei bonded to protons in the ferrocytochrome c-551 from Pseudomonas aeruginosa (ATCC 19429). Side-chain aromatic nitrogens, ma
Autor:
F, Yap-Bondoc, R, Timkovich
Publikováno v:
The Journal of biological chemistry. 265(8)
The dissimilatory nitrite reductase, cytochrome cd1, from Pseudomonas aeruginosa (ATCC 19429) was irreversibly inactivated by methyl- or phenylhydrazine but was only reduced by hydrazine itself. The reaction required oxygen and several turnovers, app
Publikováno v:
Journal of Biological Chemistry. 259:1577-1585
The substituents of the noncovalently associated heme prosthetic group of the bacterial nitrite reductase-cytochrome oxidase (EC 1.9.6.1 or EC 1.9.3.2.) from Pseudomonas aeruginosa (ATCC 19429) and Paracoccus denitrificans (ATCC 13456) have been iden
Autor:
R Timkovich, R E Dickerson
Publikováno v:
Journal of Biological Chemistry. 251:4033-4046