Abstract:
:Cytochrome c(551) from Pseudomonas aeruginosa is a monomeric redox protein of 82 amino-acid residues, involved in dissimilative denitrification as the physiological electron donor of cd(1) nitrite reductase. The distribution of charged residues on the surface of c(551) is very anisotropic: one side is richer in acidic residues whereas the other shows a ring of positive side chains, mainly lysines, located at the border of an hydrophobic patch which surrounds the heme crevice. In order to map in cytochrome c(551) the surface involved in electron transfer, we have introduced specific mutations in three residues belonging to the hydrophobic patch, namely Val23-->Asp, Pro58-->Ala and Ile59-->Glu. The effect of these mutations was analyzed studying both the self-exchange rate and the electron-transfer activity towards P. aeruginosa cd(1) nitrite reductase, the physiological partner and P. aeruginosa azurin, a copper protein often used as a model redox partner in vitro. Our results show that introduction of a negative charge in the hydrophobic patch severely hampers both homonuclear and heteronuclear electron transfer.
journal_name
J Inorg Biochemjournal_title
Journal of inorganic biochemistryauthors
Cutruzzolà F,Arese M,Ranghino G,van Pouderoyen G,Canters G,Brunori Mdoi
10.1016/s0162-0134(01)00390-7subject
Has Abstractpub_date
2002-02-01 00:00:00pages
353-61issue
3-4eissn
0162-0134issn
1873-3344pii
S0162013401003907journal_volume
88pub_type
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