Coordination geometry of haem in cyanogen bromide modified myoglobin and its effect on the formation of compound I
Abstract
By use of nuclear relaxation time measurements of the water proton, it is demonstrated unambiguously that water is not coordinated to the haem iron in BrCN-modified myoglobin; by stopped-flow measurements it is also shown that the rate of formation of compound I in the modified Mb is very similar to that in horseradish peroxidase, having similar coordination geometry.