ライフサイエンスコーパス: protoheme

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1 and then decarboxylate coproheme to generate protoheme.

2 ferrous iron into protoporphyrin IX to form protoheme.

3 moglobin (Hb), with mesoheme substituted for protoheme, allows separate monitoring of the alpha or be

4 with the corresponding rate constants of the protoheme and alpha-hydroxyheme complexes.

5 enius prefactor for CO binding to ChCooA and protoheme ( approximately 10(11) s(-1)) is similar to wh

6 The nonexponential nature of CO binding to protoheme, as well as its relaxation above the solvent g

7 This heme differs from heme B (protoheme) at two carbon positions of the porphyrin ring

8 roxyheme complex are similar to those of the protoheme complex, and hydroxylation at the alpha-meso p

9 e is dissolved in alkaline pyridine, and the protoheme concentration is estimated from a dithionite-r

10 A method for reproducibly estimating the protoheme content of plant tissues has been developed.

11 he wild type enzyme, the ferric state of the protoheme displays a mixed low spin/high spin state at r

12 The rebinding kinetics of CO to protoheme (FePPIX) in the presence and absence of a prox

13 Ferrochelatase (protoheme ferrolyase, E.C. 4.99.1.1) is the terminal enz

14 Ferrochelatase (protoheme ferrolyase, EC 4.99.1.1) is the terminal enzym

15 been generally accepted that biosynthesis of protoheme (heme) uses a common set of core metabolic int

16 ) biogenesis requires COX10, which encodes a protoheme:heme O farnesyl transferase that participates

17 Cox10p is a protoheme:heme-O-farnesyl transferase required for the s

18 eroheme (2-VDH), 4-vinyldeuteroheme (4-VDH), protoheme III (PHs), and 1-methyl-2-oxomesoheme XIII (2-

19 By comparing the rate of CO rebinding to protoheme in glycerol solution with and without a bound

20 nd to H64A or H64L Mb mutants or to chelated protoheme in soap micelles; and (3) the fraction of in c

21 n 80% acetone to remove pigments and lipids; protoheme is then extracted from the tissue residue with

22 ferrous iron into protoporphyrin IX to form protoheme, is catalyzed by the enzyme ferrochelatase (EC

23 ferrous iron into protoporphyrin IX to form protoheme IX (heme).

24 ferrous iron into protoporphyrin IX to form protoheme IX (heme).

25 ere conducted on peptides reconstituted with protoheme IX (PHa) and several related variants.

26 lymorphism in the cyoE gene, which encodes a protoheme IX farnesyltransferase, was identified.

27 When protoheme IX is incorporated, both hemes in the dimer ar

28 In addition, the enzyme binds protoheme IX, but SDH3 lacks a ligand histidine.

29 ferrous iron into protoporphyrin IX to form protoheme IX.

30 of ferrous iron into protoporphyrin to form protoheme IX.

31 of iron into the macrocycle, and release of protoheme IX.

32 rafast diatomic ligand binding to the "bare" protoheme (L(1)-FePPIX-L(2), where L(1) = H(2)O or 2-met

33 reased upon deletion of scpB or scpE and the protoheme level was reduced in the strain lacking scpE.

34 (-) control strain), whereas the PChlide and protoheme levels remained fairly constant.

35 The protoheme of Hmp binds not only O2 and NO, but also CO s

36 stitution experiments of the apoprotein with protoheme or mesoheme, we show that the nitro group is o

37 In contrast to Mb, the protoheme shows no indication of the presence of "distal

38 des of the reversed forms are assigned using protohemes that are selectively deuterated at the four m

39 he opening of the tetrapyrrole macrocycle of protoheme to form biliverdin IX alpha, in a reaction cat

40 he opening of the tetrapyrrole macrocycle of protoheme to form biliverdin IXalpha, in a reaction cata

41 tochrome c oxidase, is produced from heme B (protoheme) via two enzymatic reactions catalyzed by heme

42 the CO rebinding rate of the imidazole bound protoheme with the analogous rate in myoglobin (Mb) lead

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