199 related articles for article (PubMed ID: 3702869)
1. [Comparison of the heme electron state of reduced cytochrome P450 and P420 in equilibrium and non-equilibrium protein conformations. The nature of the protein heme ligand].
Sharonov IuA; Pis'menskiĭ VF; Greschner S; Ruckpaul K
Mol Biol (Mosk); 1986; 20(2):451-60. PubMed ID: 3702869
[TBL] [Abstract][Full Text] [Related]
2. [Electron structure of the heme of reduced cytochrome P450 and P420 from the data of low-temperature magnetic circular dichroism].
Sharonov IuA
Mol Biol (Mosk); 1986; 20(2):440-50. PubMed ID: 3702868
[TBL] [Abstract][Full Text] [Related]
3. [Absorption and magnetic circular dichroism spectra of hemoproteins in nonequilibrium states. V. Cytochrome P450 and its substrate complex].
Davydov RM; Greshner Z; Rukpaul' K
Mol Biol (Mosk); 1979; 13(6):1397-406. PubMed ID: 547182
[TBL] [Abstract][Full Text] [Related]
4. [Contribution of protein conformation to stereochemistry and reactivity of the active center of heme proteins and enzymes. The existence of horseradish peroxidase conformations and their possible role in the catalysis mechanism].
Sharonov IuA; Pis'menskiĭ VF; Iarmola EG
Mol Biol (Mosk); 1988; 22(6):1491-506. PubMed ID: 3252148
[TBL] [Abstract][Full Text] [Related]
5. [Electron-conformational interactions at the active site of reduced bacterial cytochrome P450cam induced by a substrate and analysis of the electron structure of heme].
Sharonov IuA
Mol Biol (Mosk); 1992; 26(6):1251-62. PubMed ID: 1491671
[TBL] [Abstract][Full Text] [Related]
6. Low- and ultralow-temperature magnetic circular dichroism studies of reduced cytochromes P-450-LM2 and P-420-LM2 and of photo-products of their co-complexes. The spin-state and axial ligation of heme iron.
Sharonov YuA ; Pismensky VF; Greschner S; Ruckpaul K
Biochem Biophys Res Commun; 1987 Jul; 146(1):165-72. PubMed ID: 3606614
[TBL] [Abstract][Full Text] [Related]
7. Active site analysis of P450 enzymes: comparative magnetic circular dichroism spectroscopy.
Andersson LA; Johnson AK; Peterson JA
Arch Biochem Biophys; 1997 Sep; 345(1):79-87. PubMed ID: 9281314
[TBL] [Abstract][Full Text] [Related]
8. A comparison of the heme electronic states in equilibrium and nonequilibrium protein conformations of high-spin ferrous hemoproteins. Low temperature magnetic circular dichroism studies.
Sharonov YA; Sharonova NA; Figlovsky VA; Grigorjev VA
Biochim Biophys Acta; 1982 Dec; 709(2):332-41. PubMed ID: 6295493
[TBL] [Abstract][Full Text] [Related]
9. Resonance Raman investigations of Escherichia coli-expressed Pseudomonas putida cytochrome P450 and P420.
Wells AV; Li P; Champion PM; Martinis SA; Sligar SG
Biochemistry; 1992 May; 31(18):4384-93. PubMed ID: 1581294
[TBL] [Abstract][Full Text] [Related]
10. [Absorption and magnetic circular dichroism spectra of nonequilibrium states of hemoproteins. II. Myoglobin and its complexes].
Magonov SN; Davydov RM; Bliumenfel'd LA; Vilu RO; Arutiunian AM
Mol Biol (Mosk); 1978; 12(5):1182-90. PubMed ID: 740000
[TBL] [Abstract][Full Text] [Related]
11. Engineering cytochrome c peroxidase into cytochrome P450: a proximal effect on heme-thiolate ligation.
Sigman JA; Pond AE; Dawson JH; Lu Y
Biochemistry; 1999 Aug; 38(34):11122-9. PubMed ID: 10460168
[TBL] [Abstract][Full Text] [Related]
12. Magnetic circular dichroism used to examine the interaction of Escherichia coli cytochrome bd with ligands.
Borisov V; Arutyunyan AM; Osborne JP; Gennis RB; Konstantinov AA
Biochemistry; 1999 Jan; 38(2):740-50. PubMed ID: 9888814
[TBL] [Abstract][Full Text] [Related]
13. Two enzymes with a common function but different heme ligands in the forms as isolated. Optical and magnetic properties of the heme groups in the oxidized forms of nitrite reductase, cytochrome cd1, from Pseudomonas stutzeri and Thiosphaera pantotropha.
Cheesman MR; Ferguson SJ; Moir JW; Richardson DJ; Zumft WG; Thomson AJ
Biochemistry; 1997 Dec; 36(51):16267-76. PubMed ID: 9405061
[TBL] [Abstract][Full Text] [Related]
14. Evidence for the high-spin heme iron in both stable and unstable reduced forms of lactoperoxidase: low-temperature magnetic circular dichroism data.
Sharonov YA
FEBS Lett; 1995 Dec; 377(3):512-4. PubMed ID: 8549787
[TBL] [Abstract][Full Text] [Related]
15. Identification of conformational substates involved in nitric oxide binding to ferric and ferrous myoglobin through difference Fourier transform infrared spectroscopy (FTIR).
Miller LM; Pedraza AJ; Chance MR
Biochemistry; 1997 Oct; 36(40):12199-207. PubMed ID: 9315857
[TBL] [Abstract][Full Text] [Related]
16. Modulation of protein function by exogenous ligands in protein cavities: CO binding to a myoglobin cavity mutant containing unnatural proximal ligands.
Decatur SM; DePillis GD; Boxer SG
Biochemistry; 1996 Apr; 35(13):3925-32. PubMed ID: 8672423
[TBL] [Abstract][Full Text] [Related]
17. Folding of horse cytochrome c in the reduced state.
Bhuyan AK; Udgaonkar JB
J Mol Biol; 2001 Oct; 312(5):1135-60. PubMed ID: 11580255
[TBL] [Abstract][Full Text] [Related]
18. [Absorption spectra and magnetic circular dichroism of ferrocytochrome b5 formed during low temperature reduction in a nonequilibrium state].
Davydov RM; Kariakin AV; Greshner E
Biofizika; 1980; 25(3):393-7. PubMed ID: 7397252
[TBL] [Abstract][Full Text] [Related]
19. Photochemical reactions of cytochrome oxidase at low temperatures.
Orii Y
Adv Biophys; 1978; 11():285-308. PubMed ID: 209671
[TBL] [Abstract][Full Text] [Related]
20. Resonance Raman spectroscopic identification of a histidine ligand of b595 and the nature of the ligation of chlorin d in the fully reduced Escherichia coli cytochrome bd oxidase.
Sun J; Kahlow MA; Kaysser TM; Osborne JP; Hill JJ; Rohlfs RJ; Hille R; Gennis RB; Loehr TM
Biochemistry; 1996 Feb; 35(7):2403-12. PubMed ID: 8652583
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
