Abstract:
:Nitridomanganese(V) protoporphyrin IX was prepared by hypochlorite oxidation of the corresponding manganese(III) protoporphyrin IX derivative in the presence of ammonium ion and by photolysis of the corresponding azidomanganese(III) complex. Myoglobin and horseradish peroxidase containing this novel protoporphyrin derivative were prepared for the first time. These remarkably stable species were examined by electronic absorption, electron paramagnetic resonance, and resonance Raman spectroscopies. The MnV-N stretching modes of the nitridomanganese(V)-substituted myoglobin and horseradish peroxidase were observed at 1010 and 1003 cm-1, respectively, by resonance Raman spectroscopy, while the MnV-N stretching frequency for nitridomanganese(V) protoporphyrin IX in 0.1 N aqueous NaOH was found at 1046 cm-1. The equilibrium dissociation energies of MnV-N bonds in these complexes were estimated from vibrational overtone spacings by introducing the Morse potential energy function, were found to be around 4.5 eV, and seemed independent of the surroundings of the manganese porphyrin, although its force constant decreased from 7.3 to 6.7 mdyn/A upon incorporation into apoprotein. The porphyrin ring modes of these nitridomanganese(V) derivatives were influenced greatly upon incorporation into apoproteins, suggestive of the occurrence of porphyrin core expansion. Upon this core expansion the MnV center moves into the mean plane of porphyrin plane, but the access of nitrido (N) toward MnV is restricted due to a steric hindrance from porphyrin pyrrole nitrogens. The resulting stretched MnV-N bond might cause lowering of the MnV-N stretching frequency upon incorporation into apoprotein.
journal_name
Biochemistryjournal_title
Biochemistryauthors
Tsubaki M,Hori H,Hotta T,Hiwatashi A,Ichikawa Y,Yu NTdoi
10.1021/bi00390a015subject
Has Abstractpub_date
1987-08-11 00:00:00pages
4980-6issue
16eissn
0006-2960issn
1520-4995journal_volume
26pub_type
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