Abstract:
:An iron porphycene, a structural isomer of iron porphyrin, with trifluoromethyl groups at the peripheral position of the framework was incorporated into sperm whale apomyoglobin. The prepared myoglobin shows the higher O(2) affinity than the native protein. However, the oxygen affinity of the reconstituted myoglobin is lower than that of the myoglobin having an iron porphycene without trifluoromethyl groups, which is mainly originated from the enhancement of the O(2) dissociation. The CO affinity of the myoglobin with the trifluoromethylated iron porphycene is similar to that observed for the reference protein having the iron porphycene without trifluoromethyl groups, although their C-O stretching frequencies are significantly different. The relationship between the electronic states of the porphycene ring and the ligand bindings is discussed.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Matsuo T,Ito K,Nakashima Y,Hisaeda Y,Hayashi Tdoi
10.1016/j.jinorgbio.2007.07.032subject
Has Abstractpub_date
2008-02-01 00:00:00pages
166-73issue
2eissn
0162-0134issn
1873-3344pii
S0162-0134(07)00220-6journal_volume
102pub_type
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journal_title:Journal of inorganic biochemistry
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journal_title:Journal of inorganic biochemistry
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doi:10.1016/j.jinorgbio.2015.04.006
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