ライフサイエンスコーパス: verdoheme

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1 quent O(2)-dependent fragmentation to Fe(3+)-verdoheme.

2 erobic reaction was determined to be ferrous verdoheme.

3 ed intermediates, alpha-meso-hydroxyheme and verdoheme.

4 order to produce >90% of the alpha-isomer of verdoheme.

5 isplace Met-63 from its coordination site on verdoheme.

6 pon exposure to O(2) is rapidly converted to verdoheme.

7 Thus, reduction of Fe(3+) to Fe(2+)-verdoheme (0.15 s(-1) at 4 degrees C and 0.55 s(-1) at 2

8 latter mutants retain a low ability to form verdoheme, an intermediate in the reaction sequence.

9 form with added H2O2 nor does it convert to verdoheme and CO.

10 is of aerobic reactions with H2O2 identifies verdoheme as a reaction intermediate.

11 in to biliverdin with alpha-hydroxyhemin and verdoheme as intermediates.

12 ferryl-heme as in HCO, the Cu(B)Mb generates verdoheme because the engineered Cu(B)Mb may lack a hydr

13 ic conversion of ferric alpha-hydroxyheme to verdoheme by heme oxygenase requires molecular oxygen an

14 Conversion of heme to verdoheme by heme oxygenase-1 (HO-1) is thought to invol

15 reduced in the presence of CO to the Fe(II) verdoheme-CO complex.

16 In contrast, the CO affinities of the verdoheme complexes are >10,000 times weaker than those

17 ctions with the heme, alpha-hydroxyheme, and verdoheme complexes of heme oxygenase have been studied.

18 t stage of coupled oxidation yields a stable verdoheme-containing protein.

19 xygenase complex with oxygen also yields the verdoheme-enzyme complex.

20 ge, and finally, this is the first report of verdoheme generated from a heme protein with exclusive m

21 First, the verdoheme group is covalently bound to the protein throu

22 pecies with a reducing equivalent yields the verdoheme-heme oxygenase complex.

23 a mutant (H63V) capable of oxidizing heme to verdoheme in the absence of catalase.

24 is only required to reduce ferric to ferrous verdoheme in the first step of its conversion to biliver

25 showed heme oxygenase activity by generating verdoheme in the presence of Cu(I).

26 version of alpha-meso-hydroxyheme to Fe(III) verdoheme, in contrast to a previous report, does not re

27 Much tighter binding of the inhibitor to the verdoheme intermediate differentiates it from inhibition

28 ped by coordination of the isocyanide to the verdoheme intermediate rather than to the ferric heme co

29 that the conversion of Fe(3+)-heme to Fe(3+)-verdoheme is biphasic.

30 iron(III) benzoyl-biliverdins, and the final verdoheme-like products.

31 Hydrolytic conversion of the verdoheme product to biliverdin concluded that oxidative

32 This verdoheme protein is unusual in three respects.

33 derably slow catalytic rate and low level of verdoheme recovery in the hydrogen peroxide reaction sug

34 on to a biliprotein, we demonstrate that the verdoheme ring can be opened by treatment with aqueous f

35 mu O complex with hydrogen peroxide yields a verdoheme species, the recovery of which is much less co

36 Second, the oxidation stops at the verdoheme stage, and finally, this is the first report o

37 The conversion of Fe(3+)-verdoheme to Fe(3+)-biliverdin is also biphasic.

38 mechanism of inhibition for the oxidation of verdoheme to iron-biliverdin in the H63M variant appears

39 ation is limited by the conversion of Fe(2+)-verdoheme to the Fe(3+)-biliverdin.

40 yheme-HO-1 complex with O2 generates Fe(III) verdoheme, which can be reduced in the presence of CO to

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