ライフサイエンスコーパス: hemeprotein

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1 a standard NOS heme structure as a thiolate hemeprotein.

2 O and NO were very high as compared to other hemeproteins.

3 terin and Arg to allow comparison with other hemeproteins.

4 que mechanisms of interaction between NO and hemeproteins.

5 the versatile nature by which NO can bind to hemeproteins.

6 ntral role both for characterizing different hemeproteins and their conformational states but also fo

7 the reactions of NO with ferric and ferrous hemeproteins are not as well characterized.

8 ood cells are destroyed and large amounts of hemeproteins are released.

9 ) by which it can utilize the hosts heme and hemeproteins as a source of iron.

10 monoxide; NO) reacts with the iron center of hemeproteins at near diffusion-controlled rates.

11 otected from vinyl group modification by the hemeprotein covalent bonds, we prepared the F41E mutant

12 f a transient protein radical and a covalent hemeprotein cross-link.

13 loperoxidase (MPO) is a neutrophil lysosomal hemeprotein essential for optimal oxygen-dependent micro

14 We cloned, expressed, and characterized a hemeprotein from Deinococcus radiodurans (D. radiodurans

15 Interaction of CO with hemeproteins has physiological importance.

16 Although multiple hemeproteins have been reported to function as nitrite r

17 Complex IV is the only hemeprotein in the cell that contains heme a, which may

18 eme molecule is the prosthetic group of many hemeproteins involved in essential physiological process

19 s of NO from some, not all, noniron sites in hemeproteins is very slow (t(1/2) approximately hours).

20 es oxygen when binding to the iron center of hemeproteins, leading to a reduction in blood oxygen lev

21 arbon monoxide (CO) to iron(II) sites of the hemeproteins led to evidence of NO binding to noniron, n

22 in circulation, and suggests that additional hemeproteins might be involved in sulfide homeostasis in

23 ms may utilize heme directly from the host's hemeproteins or via a hemophore that sequesters and tran

24 sion between respiratory complexes, enhances hemeprotein peroxidase and reactive oxygen species scave

25 Hemeproteins play an important role in the signaling pro

26 facilitate both thermal and photo-initiated hemeprotein reduction over large macroscopic distances.

27 yst for such reactions is myeloperoxidase, a hemeprotein secreted by activated phagocytes.

28 ential mechanism involves myeloperoxidase, a hemeprotein secreted by human phagocytes.

29 ex with heme (Kd = 2.5 +/- 1 microM) and has hemeprotein spectra similar to those previously reported

30 ults in spectral properties of the resulting hemeprotein that are consistent with the loss of a thiol

31 nducible nitric oxide synthase (iNOSox) is a hemeprotein that binds L-arginine (L-Arg) and tetrahydro

32 Human cystathionine beta-synthase is a hemeprotein that catalyzes a pyridoxal phosphate (PLP)-d

33 The latter enzyme is a unique hemeprotein that catalyzes pyridoxal phosphate (PLP)-dep

34 Cystathionine beta-synthase is a tetrameric hemeprotein that catalyzes the pyridoxal 5'-phosphate-de

35 Neuronal nitric-oxide synthase (NOS-1) is a hemeprotein that generates NO and citrulline from L-argi

36 le NO synthase (iNOS) is a flavin-containing hemeprotein that must dimerize to generate NO.

37 Inducible nitric-oxide synthase (iNOS) is a hemeprotein that requires tetrahydrobiopterin (H4B) for

38 Nitric oxide synthases (NOS) are hemeproteins that catalyze oxidation of L-arginine to ni

39 phan to N-formyl kynurenine catalyzed by two hemeproteins, tryptophan 2,3-dioxygenase (hTDO) and indo

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