Substrate binding and catalysis in heme peroxidases

Current Opinion in Chemical Biology

Volumn 2, Issue 2, 1998, Pages 269-278

  Smith, Andrew T ^a   Veitch, Nigel C ^b  

^a UNIVERSITY OF SUSSEX   (United Kingdom)

^b JODRELL LABORATORY   (United Kingdom)

Author keywords

[No Author keywords available]

Indexed keywords

FUNGAL PROTEIN; HEMOPROTEIN; PEROXIDASE; VEGETABLE PROTEIN;

BINDING SITE; CATALYSIS; CHEMICAL STRUCTURE; CHEMISTRY; KINETICS; PHYSIOLOGY; PROTEIN BINDING; PROTEIN SECONDARY STRUCTURE; REVIEW; X RAY CRYSTALLOGRAPHY;

BINDING SITES; CATALYSIS; CRYSTALLOGRAPHY, X-RAY; FUNGAL PROTEINS; HEMEPROTEINS; KINETICS; MODELS, MOLECULAR; PEROXIDASES; PLANT PROTEINS; PROTEIN BINDING; PROTEIN STRUCTURE, SECONDARY;

EID: 0032042908     PISSN: 13675931     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1367-5931(98)80069-0     Document Type: Article

References (56)

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8. •].
9. Rodriguez-Lopez JN, Smith AT, Thorneley RNF: Recombinant horseradish peroxidase isoenzyme C: the effect of distal haem cavity mutations (His42→Leu and Arg38→Leu) on compound I formation and substrate binding. J Biol Inorg Chem 1996, 1:136-142.
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11. •], but with a different emphasis. Partial restoration of catalytic activity for the largely inactive H42A HRP C mutant is achieved by the creation of a neighbouring histidine residue, rather than by addition of exogenous imidazole.
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15. Mukai M, Nagano S, Tanaka M, Ishimori K, Morishima I, Ogura T, Watanabe Y, Kitagawa T: Effects of concerted hydrogen bonding of distal histidine on active site structures of horseradish peroxidase. Resonance Raman studies with Asn70 mutants. J Am Chem Soc 1997, 119:1758-1766.
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17. 2 to HRP C, and the breaking of the O-O peroxide bond.
18. •].
19. Hill AP, Modi S, Sutcliffe MJ, Turner DD, Gilfoyle DJ, Smith AT, Tam BM, Lloyd E: Chemical, spectroscopic and structural investigation of the substrate-binding site in ascorbate peroxidase. Eur J Biochem 1997, 248:347-354.
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28. 2+ and haem. Biochem J 1996, 315:15-19.
29. 127I NMR spectroscopy, and steady-state kinetics. J Biol Chem 1997, 272:5752-5756.
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31. Itakura H, Oda Y, Fukuyama K: Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X-ray crystallographic analysis of the complex at 1.6 Å resolution. FEBS Lett 1997, 412:107-110. The first crystal structure of an enzyme from the plant peroxidase superfamily complexed to an aromatic donor molecule (Brookhaven accession code 1HSR).
32. 3 is made to Phe179 from analysis of 2D NOESY spectra.
33. 1H NMR spectra of three horseradish peroxidase isoenzymes, HRP A1, A2, and C, resulting in important new assignments for a number of key heme pocket residues. Hyperfine shift changes for the heme resonances of resting state HRP C which occur when benzhydroxamic acid is bound are interpreted to suggest that this complex is 5-c HS, rather than 6-c HS.
34. Musah RA, Goodin DB: Introduction of novel substrate oxidation into cytochrome c peroxidase by cavity complementation: Oxidation of 2-aminothiazole and covalent modification of the enzyme. Biochemistry 1997, 36:11665-11674. A highly imaginative approach is taken in this study, which extends the concept of substrate binding sites in peroxidases through creation of artificial cavities using site-directed mutagenesis. The W191G mutant of CCP is shown to bind the heterocyclic molecule, 2-aminothiazole, and to be capable of oxidising it in situ, i.e. from within the cavity.
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37. Newmyer SL, Sun J, Loehr TM, Ortiz de Montellano PR: Rescue of horseradish peroxidase His170→Ala mutant activity by imidazole: Importance of proximal ligand tethering. Biochemistry 1996, 35:12788-12795. Substitution of the proximal histidine ligand to heme iron in HRP C by Ala results in a mutant (H170A) which does not form spectroscopically detectable compound I or II intermediates. Resonance Raman spectroscopy indicates that H170A is a 6-c LS species with distal His42 coordination to heme iron. Exogenous imidazole, which binds in the resulting cavity caused by the mutation and coordinates heme iron, effectively recovers the catalytic activity of the enzyme to within 2 orders of magnitude of the wild type value. Full recovery is probably limited by the presence of the ligated distal histidine residue.
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40. Smulevich G, Neri F, Marzocchi MP, Welinder KG: Versatility of heme coordination demonstrated in a fungal peroxidase. Absorption and resonance Raman studies of Coprinus cinereus peroxidase and the Asp245→Asn mutant at various pH values. Biochemistry 1996, 35:10576-10585.
41. 1H-NMR spectroscopy and comparison with the wild-type enzyme. Biochemistry 1996, 35:14370-14380.
42. Bujons J, Dikiy A, Ferrer JC, Banci L, Mauk AG: Charge reversal of a critical active site residue of cytochrome c peroxidase. Characterization of the Arg48→Glu variant. Eur J Biochem 1997, 243:72-84.
43. Howes BD, Rodriguez-Lopez JN, Smith AT, Smulevich G: Mutations of distal residues of horseradish peroxidase: Influence on substrate binding and cavity properties. Biochemistry 1997, 36:1532-1543.
44. Rodriguez-Lopez JN, Smith AT, Thorneley RNF: Effect of distal cavity mutations on the binding and activation of oxygen by ferrous horseradish peroxidase. J Biol Chem 1997, 272:389-395.
45. Neri F, Kok D, Miller MA, Smulevich G: Fluoride binding in hemoproteins: the importance of the distal cavity structure. Biochemistry 1997, 36:8947-8953. An important paper, based on optical and resonance Raman spectroscopy, which examines subtle differences in distal pocket heme architecture within the three classes of the plant peroxidase superfamily viewed from the perspective of fluoride binding to the vacant sixth coordination site of heme iron.
46. Bonagura CA, Sundaramoorthy M, Pappa HS, Patterson WR, Poulos TL: An engineered cation site in cytochrome c peroxidase alters the reactivity of the redox active tryptophan. Biochemistry 1996, 35:6107-6115. Although the three-dimensional structures of CCP and ascorbate peroxidase are very similar, the enzymes form Trp and porphyrin cation radicals, respectively, during the catalytic cycle. This study shows that introduction of the cation binding site of APX into CCP by site-directed mutagenesis abolishes the ability of the latter to form a Trp cation radical.
47. Nie GJ, Aust SD: Spectral changes of lignin peroxidase during reversible inactivation. Biochemistry 1997, 36:5113-5119.
48. Sutherland GRJ, Zapanta LS, Tien M, Aust SD: Role of calcium in maintaining the heme environment of manganese peroxidase. Biochemistry 1997, 36:3654-3662. This study describes the structural changes which accompany thermal inactivation and calcium release in MnP. The inactive enzyme, which cannot form compound I, appears to be a 6-c LS species in which distal His acts as the sixth ligand. A distal calcium binding site mutant (D47A), constructed to minimize calcium binding affinity, exhibits similar spectroscopic properties to inactivated MnP.
49. Sutherland GRJ, Aust SD: Thermodynamics of binding of the distal calcium to manganese peroxidase. Biochemistry 1997, 36:8567-8573.
50. •].
51. Kishi K, Kusters van Someren M, Mayfield MB, Sun J, Loehr TM, Gold MH: Characterization of Mn (II) binding site mutants of manganese peroxidase. Biochemistry 1996, 35:8986-8994.
52. Sundaramoorthy M, Kishi K, Gold MH, Poulos TL: Crystal structures of substrate binding site mutants of manganese peroxidase. J Biol Chem 1997, 272:1 7574-17580. The three-dimensional structures of two manganese-binding site mutants, D179N and E35Q:D179N, are described and compared to that of wild type MnP. There is no cation present in the manganese-binding sites of these two mutants, the local structures of which are altered considerably.
53. Yeung BKS, Wang X, Sigman JA, Petillo PA, Lu Y: Construction and characterization of a manganese-binding site in cytochrome c peroxidase: toward a novel manganese peroxidase. Chem Biol 1997, 4:215-222.
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55. Tams JW, Welinder KG: Unfolding and refolding of Coprinus cinereus peroxidase at high pH, in urea, and at high temperature. Effect of organic and ionic additives on these processes. Biochemistry 1996, 35:7573-7579.
56. Henriksen A, Schuller DJ, Meno K, Welinder KG, Smith AT, Gajhede M: Structural interactions between horseradish peroxidase c and the substrate benzhydroxamic acid determined by X-ray crystallography. Biochemistry 1998, 37:in press.