267 related articles for article (PubMed ID: 7999755)
1. Spectroscopic study of Ser92 mutants of human myoglobin: hydrogen bonding effect of Ser92 to proximal His93 on structure and property of myoglobin.
Shiro Y; Iizuka T; Marubayashi K; Ogura T; Kitagawa T; Balasubramanian S; Boxer SG
Biochemistry; 1994 Dec; 33(50):14986-92. PubMed ID: 7999755
[TBL] [Abstract][Full Text] [Related]
2. Functional implications of the proximal hydrogen-bonding network in myoglobin: a resonance Raman and kinetic study of Leu89, Ser92, His97, and F-helix swap mutants.
Peterson ES; Friedman JM; Chien EY; Sligar SG
Biochemistry; 1998 Sep; 37(35):12301-19. PubMed ID: 9724545
[TBL] [Abstract][Full Text] [Related]
3. Inversion of axial coordination in myoglobin to create a "proximal" ligand binding pocket.
Uno T; Sakamoto R; Tomisugi Y; Ishikawa Y; Wilkinson AJ
Biochemistry; 2003 Sep; 42(34):10191-9. PubMed ID: 12939147
[TBL] [Abstract][Full Text] [Related]
4. Electrostatic modification of the active site of myoglobin: characterization of the proximal Ser92Asp variant.
Lloyd E; Burk DL; Ferrer JC; Maurus R; Doran J; Carey PR; Brayer GD; Mauk AG
Biochemistry; 1996 Sep; 35(36):11901-12. PubMed ID: 8794773
[TBL] [Abstract][Full Text] [Related]
5. Influence of proximal side mutations on the molecular and electronic structure of cyanomet myoglobin: an 1H NMR study.
Wu Y; Chien EY; Sligar SG; La Mar GN
Biochemistry; 1998 May; 37(19):6979-90. PubMed ID: 9578585
[TBL] [Abstract][Full Text] [Related]
6. 1H NMR study of the solution molecular and electronic structure of engineered distal myoglobin His64(E7) Val/Val68(E11) His double mutant. Coordination of His64(E11) at the sixth position in both low-spin and high-spin states.
Qin J; La Mar GN; Dou Y; Admiraal SJ; Ikeda-Saito M
J Biol Chem; 1994 Jan; 269(2):1083-90. PubMed ID: 8288565
[TBL] [Abstract][Full Text] [Related]
7. Conformational change and histidine control of heme chemistry in cytochrome c peroxidase: resonance Raman evidence from Leu-52 and Gly-181 mutants of cytochrome c peroxidase.
Smulevich G; Miller MA; Kraut J; Spiro TG
Biochemistry; 1991 Oct; 30(39):9546-58. PubMed ID: 1654102
[TBL] [Abstract][Full Text] [Related]
8. Roles of proximal ligand in heme proteins: replacement of proximal histidine of human myoglobin with cysteine and tyrosine by site-directed mutagenesis as models for P-450, chloroperoxidase, and catalase.
Adachi S; Nagano S; Ishimori K; Watanabe Y; Morishima I; Egawa T; Kitagawa T; Makino R
Biochemistry; 1993 Jan; 32(1):241-52. PubMed ID: 8380334
[TBL] [Abstract][Full Text] [Related]
9. Electron-nuclear coupling to the proximal histidine in oxy cobalt-substituted distal histidine mutants of human myoglobin.
Lee HC; Peisach J; Dou Y; Ikeda-Saito M
Biochemistry; 1994 Jun; 33(24):7609-18. PubMed ID: 8011627
[TBL] [Abstract][Full Text] [Related]
10. Alteration of axial coordination by protein engineering in myoglobin. Bisimidazole ligation in the His64-->Val/Val68-->His double mutant.
Dou Y; Admiraal SJ; Ikeda-Saito M; Krzywda S; Wilkinson AJ; Li T; Olson JS; Prince RC; Pickering IJ; George GN
J Biol Chem; 1995 Jul; 270(27):15993-6001. PubMed ID: 7608158
[TBL] [Abstract][Full Text] [Related]
11. Preparation and reactions of myoglobin mutants bearing both proximal cysteine ligand and hydrophobic distal cavity: protein models for the active site of P-450.
Matsui T; Nagano S; Ishimori K; Watanabe Y; Morishima I
Biochemistry; 1996 Oct; 35(40):13118-24. PubMed ID: 8855949
[TBL] [Abstract][Full Text] [Related]
12. 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]
13. Computer modelling of dynamics of Ser92X deoxymyoglobin mutants.
Nowak W
Comput Chem; 1998; 22(1):49-59. PubMed ID: 9570112
[TBL] [Abstract][Full Text] [Related]
14. Replacement of the proximal ligand of sperm whale myoglobin with free imidazole in the mutant His-93-->Gly.
Barrick D
Biochemistry; 1994 May; 33(21):6546-54. PubMed ID: 8204590
[TBL] [Abstract][Full Text] [Related]
15. Phe-46(CD4) orients the distal histidine for hydrogen bonding to bound ligands in sperm whale myoglobin.
Lai HH; Li T; Lyons DS; Phillips GN; Olson JS; Gibson QH
Proteins; 1995 Aug; 22(4):322-39. PubMed ID: 7479707
[TBL] [Abstract][Full Text] [Related]
16. Ligand binding properties of myoglobin reconstituted with iron porphycene: unusual O2 binding selectivity against CO binding.
Matsuo T; Dejima H; Hirota S; Murata D; Sato H; Ikegami T; Hori H; Hisaeda Y; Hayashi T
J Am Chem Soc; 2004 Dec; 126(49):16007-17. PubMed ID: 15584735
[TBL] [Abstract][Full Text] [Related]
17. Proximal ligand control of heme iron coordination structure and reactivity with hydrogen peroxide: investigations of the myoglobin cavity mutant H93G with unnatural oxygen donor proximal ligands.
Roach MP; Puspita WJ; Watanabe Y
J Inorg Biochem; 2000 Aug; 81(3):173-82. PubMed ID: 11051562
[TBL] [Abstract][Full Text] [Related]
18. Serine92 (F7) contributes to the control of heme reactivity and stability in myoglobin.
Smerdon SJ; Krzywda S; Wilkinson AJ; Brantley RE; Carver TE; Hargrove MS; Olson JS
Biochemistry; 1993 May; 32(19):5132-8. PubMed ID: 8494890
[TBL] [Abstract][Full Text] [Related]
19. Alteration of sperm whale myoglobin heme axial ligation by site-directed mutagenesis.
Egeberg KD; Springer BA; Martinis SA; Sligar SG; Morikis D; Champion PM
Biochemistry; 1990 Oct; 29(42):9783-91. PubMed ID: 2176857
[TBL] [Abstract][Full Text] [Related]
20. Engineering peroxidase activity in myoglobin: the haem cavity structure and peroxide activation in the T67R/S92D mutant and its derivative reconstituted with protohaemin-l-histidine.
Roncone R; Monzani E; Murtas M; Battaini G; Pennati A; Sanangelantoni AM; Zuccotti S; Bolognesi M; Casella L
Biochem J; 2004 Feb; 377(Pt 3):717-24. PubMed ID: 14563209
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]
