title: Coordination modes of tyrosinate-ligated catalase-type heme enzymes: magnetic circular dichroism studies of Plexaura homomalla allene oxide synthase, Mycobacterium avium ssp. paratuberculosis protein-2744c, and bovine liver catalase in their ferric and ferrous states.
abstract: Bovine liver catalase (BLC), catalase-related allene oxide synthase (cAOS) from Plexaura homomalla, and a recently isolated protein from the cattle pathogen Mycobacterium avium ssp. paratuberculosis (MAP-2744c (MAP)) are all tyrosinate-ligated heme enzymes whose crystal structures have been reported. cAOS and MAP have low (<20%) sequence similarity to, and significantly different catalytic functions from, BLC. cAOS transforms 8R-hydroperoxy-eicosatetraenoic acid to an allene epoxide, whereas the MAP protein is a putative organic peroxide-dependent peroxidase. To elucidate factors influencing the functions of these and related heme proteins, we have investigated the heme iron coordination properties of these tyrosinate-ligated heme enzymes in their ferric and ferrous states using magnetic circular dichroism and UV-visible absorption spectroscopy. The MAP protein shows remarkable spectral similarities to cAOS and BLC in its native Fe(III) state, but clear differences from ferric proximal heme ligand His93Tyr Mb (myoglobin) mutant, which may be attributed to the presence of an Arg(+)-N(ω)-H···¯O-Tyr (proximal heme axial ligand) hydrogen bond in the first three heme proteins. Furthermore, the spectra of Fe(III)-CN¯, Fe(III)-NO, Fe(II)-NO (except for five-coordinate MAP), Fe(II)-CO, and Fe(II)-O(2) states of cAOS and MAP, but not H93Y Mb, are also similar to the corresponding six-coordinate complexes of BLC, suggesting that a tyrosinate (Tyr-O¯) is the heme axial ligand trans to the bound ligands in these complexes. The Arg(+)-N(ω)-H to ¯O-Tyr hydrogen bond would be expected to modulate the donor properties of the proximal tyrosinate oxyanion and, combined with the subtle differences in the catalytic site structures, affect the activities of cAOS, MAP and BLC.
authors: Department of Chemistry and Biochemistry, University of South Carolina, Columbia, SC 29208, USA.
authors: D M Indika
authors: DM
authors: Bandara
authors: Masanori
authors: M
authors: Sono
authors: Grant S
authors: GS
authors: Bruce
authors: Alan R
authors: AR
authors: Brash
authors: John H
authors: JH
authors: Dawson
mesh_terms: D019943:Amino Acid Substitution; D000818:Animals; D037421:Anthozoa / Q000201:enzymology*; D001426:Bacterial Proteins / Q000737:chemistry*; D002248:Carbon Monoxide / Q000737:chemistry; D002374:Catalase / Q000737:chemistry*; D020134:Catalytic Domain; D002417:Cattle; D002942:Circular Dichroism; D056831:Coordination Complexes / Q000737:chemistry; D005290:Ferric Compounds / Q000737:chemistry; D005296:Ferrous Compounds / Q000737:chemistry; D006801:Humans; D006860:Hydrogen Bonding; D007501:Iron / Q000737:chemistry*; D008084:Lipoxygenase / Q000737:chemistry*; D008099:Liver / Q000201:enzymology*; D016927:Mycobacterium avium subsp. paratuberculosis / Q000201:enzymology*; D009211:Myoglobin / Q000737:chemistry / Q000235:genetics; D010084:Oxidation-Reduction; D010544:Peroxidases / Q000737:chemistry*
chemical_list: D001426:Bacterial Proteins; D056831:Coordination Complexes; D005290:Ferric Compounds; D005296:Ferrous Compounds; D009211:Myoglobin; D002248:Carbon Monoxide; D007501:Iron; D010544:Peroxidases; D002374:Catalase; D008084:Lipoxygenase; C108279:Allene oxide synthase-lipoxygenase protein, Plexaura homomalla