| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
|
|
|
|||||||
|
|||||||||
J. Biol. Chem., Vol. 255, Issue 17, 8050-8053, Sep, 1980
RJ Morris and QH Gibson
The Root effect hemoglobin from Thunnus thynnus, the Atlantic bluefin tuna,
remains in the T state at acid pH even when liganded. There are two
components in the binding of CO to the T state with rates of 0.01 and 1.0 X
10(6) M-1 S-1 at 20 degrees C, 0.1 M KPi, pH 6.0, and two components in
binding to the R state with rates of 1.7 and 8.5 X 10(6) M-1 S-1 as
measured by partial flash photolysis at 20 degrees C, 0.05 M Tris-HCl, pH
8.0. A single rate of NO binding of 1.8 X 10(7) M-1 S-1 is found at both pH
6 and pH 8. The rate of binding of NO to dimethyldeuterohemedisulfonate is
much higher still at 5 X 10(8) M-1 S- 1. The observed rate of NO binding to
the protein is not affected by chain differences or by the R to T
transition. It may measure the rate of diffusion of ligand to the vicinity
of the heme site. The T state components have different NO dissociation
velocity constants of 0.004 and 0.07 S-1. The apparent quantum yields for
the T state components are approximately 0.035 and 0.0008; the high
affinity component has the lower yield. A two-step scheme is used to
explain the results. The presence of chain differences and allosteric
states is reflected in the intrinsic binding rates of both NO and CO to the
heme group.
The role of diffusion in limiting the rate of ligand binding to hemoglobin
CiteULike 
Complore 
Connotea 
Del.icio.us 
Digg 
Reddit 
Technorati What's this?
This article has been cited by other articles:
|
|
 |
|
  A. B. Blood and G. G. Power In vitro and in vivo kinetic handling of nitrite in blood: effects of varying hemoglobin oxygen saturation Am J Physiol Heart Circ Physiol, September 1, 2007; 293(3): H1508 - H1517. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 R. Grubina, Z. Huang, S. Shiva, M. S. Joshi, I. Azarov, S. Basu, L. A. Ringwood, A. Jiang, N. Hogg, D. B. Kim-Shapiro, et al. Concerted Nitric Oxide Formation and Release from the Simultaneous Reactions of Nitrite with Deoxy- and Oxyhemoglobin J. Biol. Chem., April 27, 2007; 282(17): 12916 - 12927. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. B. Kim-Shapiro, A. N. Schechter, and M. T. Gladwin Unraveling the Reactions of Nitric Oxide, Nitrite, and Hemoglobin in Physiology and Therapeutics Arterioscler. Thromb. Vasc. Biol., April 1, 2006; 26(4): 697 - 705. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 I. B. Perillo, R. W. Hyde, A. J. Olszowka, A. P. Pietropaoli, L. M. Frasier, A. Torres, P. T. Perkins, R. E. Forster II, M. J. Utell, and M. W. Frampton Chemiluminescent measurements of nitric oxide pulmonary diffusing capacity and alveolar production in humans J Appl Physiol, November 1, 2001; 91(5): 1931 - 1940. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 Y. Zhao, P. E. Brandish, D. P. Ballou, and M. A. Marletta A molecular basis for nitric oxide sensing by soluble guanylate cyclase PNAS, December 21, 1999; 96(26): 14753 - 14758. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
C. Bonaventura, J. Bonaventura, D. T.-b. Shih, E. T. Iben, and J. Friedman Altered Ligand Rebinding Kinetics Due to Distal-side Effects in Hemoglobin Chico (Lysbeta 66(E10) right-arrow Thr) J. Biol. Chem., March 26, 1999; 274(13): 8686 - 8693. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
A. S. Rudolph, A. Sulpizio, P. Hieble, V. Macdonald, M. Chavez, and G. Feuerstein Liposome encapsulation attenuates hemoglobin-induced vasoconstriction in rabbit arterial segments J Appl Physiol, June 1, 1997; 82(6): 1826 - 1835. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 J. Friedman Structure, dynamics, and reactivity in hemoglobin Science, June 14, 1985; 228(4705): 1273 - 1280. [Abstract] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
| All ASBMB Journals | Molecular and Cellular Proteomics |
| Journal of Lipid Research | ASBMB Today |
