Electron transfer between cytochrome b(5) and some oxidised haemoglobins: the role of ionic strength.
We have compared experimental measurements and Brownian dynamic calculations for the reduction of oxidised adult human haemoglobin by reduced bovine cytochrome b(5) over a range of ionic strengths. Our calculations suggest that the presence of molecular electrostatic fields have a significant role to play in the formation of the electron transfer complexes. These results predict that electron transfer occurs within an ensemble of similarly weakly docked complexes, the formation of which is strongly ionic strength dependent. Application of electron tunneling analysis to the complexes allows us to predict the rates of electron transfer within each ensemble of complexes as a function of ionic strength. The outcome of this theoretical study is compared with experimental rate measurements. A comparison of the results obtained from adult and embryonic haemoglobins, at a fixed ionic strength, indicates a significant difference in the characteristics of complex formation. These data emphasise the role played by electrostatic interactions in this important physiological reaction.
Brittain
Thomas
T
School of Biological Science, Private Bag 92019, University of Auckland, Auckland, New Zealand. t.brittain@auckland.acv.nz
Kidd
Richard D
RD
Baker
Edward N
EN
D000818:Animals; D002417:Cattle; D003198:Computer Simulation; D015786:Cytochromes b5 / Q000737:chemistry*; D006454:Hemoglobins / Q000737:chemistry*; D006801:Humans; D007700:Kinetics; D008706:Methemoglobin / Q000737:chemistry*; D008954:Models, Biological; D009994:Osmolar Concentration; D010084:Oxidation-Reduction
D006454:Hemoglobins; D008706:Methemoglobin; D015786:Cytochromes b5