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1 roximal Trp is important in the oxidation of ferrocytochrome c.
2 ochrome c that yields ferricytochrome b5 and ferrocytochrome c.
3 ain and side chain dynamics in R. capsulatus ferrocytochrome c(2) derived from (2)H NMR relaxation of
4 ts obtained indicate that the side chains of ferrocytochrome c(2) exhibit a wide range of motional am
5 arlier results indicating that R. capsulatus ferrocytochrome c(2) exhibits minor rotational anisotrop
6 The effects of the mutations on oxidation of ferrocytochrome c and 2,6-dimethoxyphenol were also exam
7 dase have been probed by reduction with both ferrocytochrome c and acetylpyridine NADH under anaerobi
8 ectron transfer reactions between ferri- and ferrocytochrome c and N,N,N',N'-tetramethylphenylenediam
11 olutions composed of mixtures of diamagnetic ferrocytochrome c and paramagnetic ferricytochrome c.
12 Two-dimensional spectra of the complex of ferrocytochrome c and plastocyanin were screened systema
13 r electron transfer between the cross-linked ferrocytochrome c and the Trp-191 cation radical site in
14 The activity of the cation mutants using ferrocytochrome c as a substrate is < 1% of wild type le
15 covalent complex oxidizes exogenously added ferrocytochrome c at a slow rate (t(1/2) approximately 2
16 st, complex 2 is inactive toward horse heart ferrocytochrome c at all ionic strengths tested and yeas
17 nteraction of CCP with horse heart and yeast ferrocytochrome c at high ionic strengths is blocked.
19 y hydrogen peroxide, demonstrating that only ferrocytochrome c bound at the Pelletier-Kraut site is o
20 ady-state oxidation of exogenous yeast iso-1-ferrocytochrome c by hydrogen peroxide, demonstrating th
23 librium data show that the high stability of ferrocytochrome c can be rationalized as a requirement t
24 NO sensor soluble guanylate cyclase, and the ferrocytochrome c/cardiolipin complex have led to the su
25 a significant rate in the presence of either ferrocytochrome c (Cc2+) or Cc3+, indicating it is not s
26 stopped flow methods, the rate at which the ferrocytochrome c covalently attached to the peroxidase
27 ic strengths and low concentrations of yeast ferrocytochrome c does complex 2 give wild type enzyme a
28 ing that reduction of the guanine radical by ferrocytochrome c does not compete effectively with cros
29 bstitutions that occur during the folding of ferrocytochrome c [Fe(II)cyt c] have been monitored by t
30 c by either zinc-substituted cytochrome c or ferrocytochrome c has led to the estimation of a Kd for
31 denaturant-induced unfolding equilibrium of ferrocytochrome c in the presence and in the absence of
32 an electron conduit shuttling electrons from ferrocytochrome c into the hydrophobic core of the enzym
33 type enzyme when either horse heart or yeast ferrocytochrome c is used as an exogenous substrate, ind
34 P compound I and its mixing with horse heart ferrocytochrome c is varied, show that the stability of
37 of Saccharomyces cerevisiae iso-1-ferri- and ferrocytochromes c were studied using equilibrium and ki
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