ライフサイエンスコーパス: cytochrome c2

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1 t-dependent manner at a much lower rate than cytochrome c2.

2 proteins (HiPIPs) (PioC and Rpal_4085) and a cytochrome c2.

3 ts for the binding of Rhodobacter capsulatus cytochrome c2 and its K93P mutant to the cytochrome bc1

4 wing that CcmI does not interact with mature cytochrome c2 and that heme converts apocytochrome c2 in

5 separate sites or conformations of oxidized cytochrome c2 and/or cytochrome bc1.

6 ds near the heme of cytochrome c1, while the cytochrome c2 binding site is also near the cytochrome c

7 high affinity (Kd = 0.06 microM) and reduced cytochrome c2 binds less strongly (Kd = 0.11 microM) but

8 In contrast, oxidized cytochrome c2 binds to oxidized cytochrome bc1 in a biph

9 sence of stigmatellin, we find that oxidized cytochrome c2 binds to oxidized cytochrome bc1 in a mono

10 d to Ps+ growth by cycA encoding the soluble cytochrome c2 but was unable to produce several c-type c

11 demonstrate that RegA controls expression of cytochromes c2, c(y) and the cytochrome bc1 complex that

12 1; chloroplast cytochromes c6, cf; bacterial cytochromes c2, c550, c551; in total 164 sequences) have

13 he opposite side from the Rieske site, where cytochrome c2 cannot directly interact with Rieske.

14 native histidine ligation are avoided, since cytochrome c2 contains only one histidine, His17, which

15 pts were detected in vitro for R. capsulatus cytochrome c2 (cycA) and fructose-inducible (fruB) promo

16 iously characterized mobile electron carrier cytochrome c2 (cyt c2) and the more recently discovered

17 ium Rhodobacter sphaeroides, a water soluble cytochrome c2 (cyt c2) is the electron donor to the reac

18 n center (RC) of Rhodobacter sphaeroides and cytochrome c2 (cyt c2), its physiological secondary elec

19 Rhodobacter sphaeroides strains lacking cytochrome c2 (cyt c2), the normal electron donor to P87

20 Cytochrome c2 (cyt) is the mobile electron donor to the

21 tudy provides an all-atom description of the cytochrome c2-docked bc1 complex in Rhodobacter sphaeroi

22 hI-cycI) that also encodes an isoform of the cytochrome c2 family of electron transport proteins (iso

23 In spite of marginal sequence homology, cytochrome c2 from photosynthetic bacteria and the mitoc

24 rements of the folding/unfolding reaction of cytochrome c2 from Rhodobacter capsulatus were performed

25 P1 promoter for the Rhodobacter sphaeroides cytochrome c2 gene (cycA).

26 on of the peroxynitrite-induced oxidation of cytochrome c2+, hydroxylation of benzoate, and nitration

27 components of the soluble electron carrier (cytochrome c2)-independent photosynthetic (Ps) growth pa

28 inearly transfers electrons from iron, while cytochrome c2 is required for cyclic electron flow.

29 oguanidine neither affected the oxidation of cytochrome c2+ nor reacted with ground state peroxynitri

30 Deleting the gene encoding cytochrome c2 resulted in a loss of photosynthetic abili

31 se results are consistent with R. capsulatus cytochrome c2 stabilizing the complex through hydrogen b

32 a Ps- mutant (FJM13) was isolated from a Ps+ cytochrome c2-strain.

33 The reduced form of cytochrome c2 strongly binds to reduced cytochrome bc1 (

34 operon, and from cycA P3, a promoter for the cytochrome c2 structural gene.

35 e to eight mutants of Rhodobacter capsulatus cytochrome c2 that differ in overall protein stability.

36 responsible for biphasic binding of oxidized cytochrome c2 to cytochrome c1.

37 endent methods: a functional assay involving cytochrome c2 to measure the rate of QA-. oxidation, opt

38 series of conformational changes that allow cytochrome c2 to recognize the bc1 complex and bind or u

39 d minimizing binding of the product, reduced cytochrome c2, when it is proximal to cytochrome c1.

40 aximizing binding of the substrate, oxidized cytochrome c2, when the iron-sulfur cluster is proximal

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