Abstract：
:Catalytic mechanisms of reduction of O(2) to 2H(2)O by respiratory terminal oxidases have been extensively investigated. Tri-heme (b(558), b(595), d) cytochrome bd oxidases presumably utilize a dihemic site composed of high-spin hemes d and b(595). We performed a CO photolysis/recombination study of the purified fully reduced cytochrome bd from Escherichia coli. Spectrum of CO photolysis suggests photodissociation of the ligand from heme d and from part of heme b(595). This is the first clear evidence of interaction of heme b(595) with CO at room temperature. The amount of the heme d-CO species is higher after recombination than before photolysis. In the enzyme population with heme b(595) bound to CO, heme d remains unliganded, hence the dihemic O(2)-reducing pocket in cytochrome bd can bind one rather than two diatomic molecules. Occupancy of the site by one ligand molecule probably blocks access of a second molecule. Thus cytochrome bd exhibits strong negative cooperativity in ligand binding. Immediately after photolysis/recombination CO occupies 100% of the heme d sites, whereas after equilibration, the ligand gets located at heme d in 90-95% and at heme b(595) in 5-10% of the cytochrome. The equilibration process is possibly associated with an exchange of heme d endogenous ligand.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Borisov VB,Verkhovsky MIdoi
10.1016/j.jinorgbio.2012.09.016subject
Has Abstractpub_date
2013-01-01 00:00:00pages
65-7eissn
0162-0134issn
1873-3344pii
S0162-0134(12)00304-2journal_volume
118pub_type
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