Microperoxidase-11: molecular dynamics and Q-band excited resonance Raman of the oxidized, reduced and carbonyl forms.
Resonance Raman spectra with Q-band excitation are reported for microperoxidase-11, the cytochrome c analog. Spectra were acquired in the mid-frequency range for the oxidized, and reduced forms of the undecapeptide, as well as for the imidazole and carbonyl complexes. Oxidation and spin state marker bands of the undecapeptides are consistent with a six-coordinate, low spin iron in both oxidation states. Porphyrin core size correlations yield a porphyrin-centre to pyrrole-nitrogen distance of 2.00 A for MP11, suggestive of a six-coordinate species in a distorted heme environment. Molecular dynamics results show that the non-planarity of the heme of the parent cytochrome is conserved in the microperoxidase and its carbonmonoxy analog.
Laberge
M
M
Johnson Research Foundation, Department of Biochemistry & Biophysics, University of Pennsylvania, Philadelphia 19104, USA. labergem@mail.med.upenn.edu
Vreugdenhil
A J
AJ
Vanderkooi
J M
JM
Butler
I S
IS
D002248:Carbon Monoxide; D003574:Cytochrome c Group / Q000737:chemistry; D008958:Models, Molecular; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry*; D013059:Spectrum Analysis, Raman
D003574:Cytochrome c Group; D002248:Carbon Monoxide; D010544:Peroxidases; C021799:microperoxidase