318 related articles for article (PubMed ID: 7827072)
1. Evidence for sub-picosecond heme doming in hemoglobin and myoglobin: a time-resolved resonance Raman comparison of carbonmonoxy and deoxy species.
Franzen S; Bohn B; Poyart C; Martin JL
Biochemistry; 1995 Jan; 34(4):1224-37. PubMed ID: 7827072
[TBL] [Abstract][Full Text] [Related]
2. Structural heterogeneity of the Fe(2+)-N epsilon (HisF8) bond in various hemoglobin and myoglobin derivatives probed by the Raman-active iron histidine stretching mode.
Gilch H; Schweitzer-Stenner R; Dreybrodt W
Biophys J; 1993 Oct; 65(4):1470-85. PubMed ID: 8274641
[TBL] [Abstract][Full Text] [Related]
3. Functional aspects of ultra-rapid heme doming in hemoglobin, myoglobin, and the myoglobin mutant H93G.
Franzen S; Bohn B; Poyart C; DePillis G; Boxer SG; Martin JL
J Biol Chem; 1995 Jan; 270(4):1718-20. PubMed ID: 7829506
[TBL] [Abstract][Full Text] [Related]
4. Identification of histidine 77 as the axial heme ligand of carbonmonoxy CooA by picosecond time-resolved resonance Raman spectroscopy.
Uchida T; Ishikawa H; Ishimori K; Morishima I; Nakajima H; Aono S; Mizutani Y; Kitagawa T
Biochemistry; 2000 Oct; 39(42):12747-52. PubMed ID: 11041838
[TBL] [Abstract][Full Text] [Related]
5. Absorption band III kinetics probe the picosecond heme iron motion triggered by nitric oxide binding to hemoglobin and myoglobin.
Yoo BK; Kruglik SG; Lamarre I; Martin JL; Negrerie M
J Phys Chem B; 2012 Apr; 116(13):4106-14. PubMed ID: 22394099
[TBL] [Abstract][Full Text] [Related]
6. Picosecond resonance Raman evidence for unrelaxed heme in the (carbonmonoxy)myoglobin photoproduct.
Dasgupta S; Spiro TG; Johnson CK; Dalickas GA; Hochstrasser RM
Biochemistry; 1985 Sep; 24(20):5295-7. PubMed ID: 4074696
[TBL] [Abstract][Full Text] [Related]
7. Heme photolysis occurs by ultrafast excited state metal-to-ring charge transfer.
Franzen S; Kiger L; Poyart C; Martin JL
Biophys J; 2001 May; 80(5):2372-85. PubMed ID: 11325737
[TBL] [Abstract][Full Text] [Related]
8. Spectroscopic studies of myoglobin at low pH: heme ligation kinetics.
Sage JT; Li PS; Champion PM
Biochemistry; 1991 Feb; 30(5):1237-47. PubMed ID: 1991103
[TBL] [Abstract][Full Text] [Related]
9. Heme-CO religation in photolyzed hemoglobin: a time-resolved Raman study of the Fe-CO stretching mode.
Schneebeck MC; Vigil LE; Friedman JM; Chavez MD; Ondrias MR
Biochemistry; 1993 Feb; 32(5):1318-23. PubMed ID: 8448140
[TBL] [Abstract][Full Text] [Related]
10. Time-resolved resonance Raman study on ultrafast structural relaxation and vibrational cooling of photodissociated carbonmonoxy myoglobin.
Kitagawa T; Haruta N; Mizutani Y
Biopolymers; 2002; 67(4-5):207-13. PubMed ID: 12012433
[TBL] [Abstract][Full Text] [Related]
11. Spectroscopic and functional characterization of T state hemoglobin conformations encapsulated in silica gels.
Samuni U; Dantsker D; Juszczak LJ; Bettati S; Ronda L; Mozzarelli A; Friedman JM
Biochemistry; 2004 Nov; 43(43):13674-82. PubMed ID: 15504030
[TBL] [Abstract][Full Text] [Related]
12. Resonance Raman spectra of photodissociated carbonmonoxy hemoglobin and deoxy hemoglobin at 10 K.
Ondrias MR; Rousseau DL; Simon SR
J Biol Chem; 1983 May; 258(9):5638-42. PubMed ID: 6853537
[TBL] [Abstract][Full Text] [Related]
13. Picosecond primary structural transition of the heme is retarded after nitric oxide binding to heme proteins.
Kruglik SG; Yoo BK; Franzen S; Vos MH; Martin JL; Negrerie M
Proc Natl Acad Sci U S A; 2010 Aug; 107(31):13678-83. PubMed ID: 20643970
[TBL] [Abstract][Full Text] [Related]
14. A photolysis-triggered heme ligand switch in H93G myoglobin.
Franzen S; Bailey J; Dyer RB; Woodruff WH; Hu RB; Thomas MR; Boxer SG
Biochemistry; 2001 May; 40(17):5299-305. PubMed ID: 11318654
[TBL] [Abstract][Full Text] [Related]
15. Investigations of optical line shapes and kinetic hole burning in myoglobin.
Srajer V; Champion PM
Biochemistry; 1991 Jul; 30(30):7390-402. PubMed ID: 1854744
[TBL] [Abstract][Full Text] [Related]
16. UV resonance Raman studies of alpha-nitrosyl hemoglobin derivatives: relation between the alpha 1-beta 2 subunit interface interactions and the Fe-histidine bonding of alpha heme.
Nagatomo S; Nagai M; Tsuneshige A; Yonetani T; Kitagawa T
Biochemistry; 1999 Jul; 38(30):9659-66. PubMed ID: 10423244
[TBL] [Abstract][Full Text] [Related]
17. The 1.9 A structure of deoxy beta 4 hemoglobin. Analysis of the partitioning of quaternary-associated and ligand-induced changes in tertiary structure.
Borgstahl GE; Rogers PH; Arnone A
J Mol Biol; 1994 Feb; 236(3):831-43. PubMed ID: 8114097
[TBL] [Abstract][Full Text] [Related]
18. 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]
19. Transient Raman study of hemoglobin: structural dependence of the iron-histidine linkage.
Friedman JM; Rousseau DL; Ondrias MR; Stepnoski RA
Science; 1982 Dec; 218(4578):1244-6. PubMed ID: 7146910
[TBL] [Abstract][Full Text] [Related]
20. A possible allosteric communication pathway identified through a resonance Raman study of four beta37 mutants of human hemoglobin A.
Peterson ES; Friedman JM
Biochemistry; 1998 Mar; 37(13):4346-57. PubMed ID: 9521755
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]