Primary compounds of catalase and peroxidase

Brill, Arthur S.; Williams, R. J. P.

doi:10.1042/bj0780253

Cited by 103 publications

(64 citation statements)

References 13 publications

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“…High spin ferric hemes give two characteristic CT bands that produce derivative-shaped features in the MCD spectrum (15,16). The higher energy band is seen in the 600 -700-nm region, and its precise wavelength is sensitive to the nature of the axial ligands (Table I).…”

Section: Resultsmentioning

confidence: 99%

Spectral Properties of Bacterial Nitric-oxide Reductase

Field¹,

Prior²,

Roldán³

et al. 2002

Journal of Biological Chemistry

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Bacterial nitric-oxide reductase catalyzes the two electron reduction of nitric oxide to nitrous oxide. In the oxidized form the active site non-heme Fe B and high spin heme b 3 are -oxo bridged. The heme b 3 has a ligand-to-metal charge transfer band centered at 595 nm, which is insensitive to pH over the range of 6.0 -8.5. Partial reduction of nitric-oxide reductase yields a three electron-reduced state where only the heme b 3 remains oxidized. This results in a shift of the heme b 3 charge transfer band max to longer wavelengths. At pH 6.0 the charge transfer band max is 605 nm, whereas at pH 8.5 it is 635 nm. At pH 6.5 and 7.5 the nitric-oxide reductase ferric heme b 3 population is a mixture of both 605-and 635-nm forms. Magnetic circular dichroism spectroscopy suggests that at all pH values examined the proximal ligand to the ferric heme b 3 in the three electronreduced form is histidine. At pH 8.5 the distal ligand is hydroxide, whereas at pH 6.0, when the enzyme is most active, it is water.

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Section: Resultsmentioning

confidence: 99%

Spectral Properties of Bacterial Nitric-oxide Reductase

Field¹,

Prior²,

Roldán³

et al. 2002

Journal of Biological Chemistry

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“…This NMR evidence supports the direct binding of formate to the heme iron. Yet such a question may be evoked that the external ligand might not directly coordinate to the heme iron, instead it is only perturbing the mode of interaction between the unsubstituted water molecule and the heine iron, and that the changes in the hyperfine-shifted heme methyl resonance and visible absorption spectrum of the formate complex [3] might be secondary responses. However, such a possibility can be ruled out by the following analysis.…”

Section: Resultsmentioning

confidence: 99%

Proton nuclear magnetic resonance study of formate binding to metmyoglobin

Morishima¹,

Neya²,

Ogawa³

et al. 1977

FEBS Letters

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“…Early investigations indicated that these compounds could be formed from alkyl (3, 4) and acyl hydroperoxides (5) as well as several inorganic oxidizing agents (6). A variety of possibie structures has been proposed for these compounds (7)(8)(9)(10). Recently, it has been shown that oxygen is incorporated into compound I of ch!oroperoxidase upon its formation from m-chloroperbenzoic acid (11,12).…”

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confidence: 99%

Studies on Horseradish Peroxidase. XI. On the Nature of Compounds I and II as Determined from the Kinetics of the Oxidation of Ferrocyanide

Cotton¹,

Dunford²

1973

Can. J. Chem.

269

109

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In order to investigate the nature of compounds I and I1 of horseradish peroxidase, the kinetics were studied of ferrocyanide oxidation catalyzed by these compounds which were prepared from three different oxidizing agents. The p H dependence of the apparent second-order rate constant for ferrocyanide oxidation by compound I, prepared from ethyl hydroperoxide and m-chloroperbenzoic acid, was interpreted in terms of an ionization on the enzyme with a pK, = 5.3, identical to that reported previously for hydrogen peroxide. The second-order rate constant for the compound 11-ferrocyanide reaction also showed the same p H dependence for the three oxidizing substrates. However, with more accurate results, the compound 11-ferrocyanide reaction was reinterpreted in terms of a single ionization with pK, = 8.5. The same dependence of ferrocyanide oxidation on p H suggests structurally identical active sites for compounds I and I1 prepared from the three different oxidizing substrates.Pour etudier la nature des composes I et I1 de la peroxydase de raifort, on a examine les cinetiques de l'oxydation du ferrocyanure catalysee par ces composes, qui ont ete prepares a partir de trois agents oxydants differents. L'influence du p H sur la constante de vitesse apparente du deuxieme ordre poul l'oxydation du ferrocyanure par le compose I prepare a partir de I'hydroperoxyde d'ethyle et de l'acide nz-chloroperbenzoique, a ete interpretee en fonction de I'ionisation de I'enzyme a un pK, = 5.3, identique a celle precedemrnent rapportee pour I'eau oxygenee. La constante de vitesse du second ordre pour la reaction entre le ferrocyanure et le compose 11, montre aussi la mCme relation de p H pour les trois substrats oxydants. Cependant, avec des risultats plus precis, la reaction entre le ferrocyanure et le compose I1 a ete reinterprktee par rapport a l'ionisation simple a pK, = 8.5. La mCme relation entre I'oxydation du ferrocyanure et le p H laisse penser a des sites actifs de structure identique pour les composts I et TI, prepares a partir de trois substrats oxydants differents.[Traduit par le journal]Can. J. Chern.. 51. 582 (1973) The intermediate compounds of horseradish peroxidase (HRP), that is, compound I (HRP-I) and compound PI (HRP-II), have been known for many years (1, 2). Early investigations indicated that these compounds could be formed from alkyl (3, 4) and acyl hydroperoxides (5) as well as several inorganic oxidizing agents (6). A variety of possibie structures has been proposed for these compounds (7)(8)(9)(10). Recently, it has been shown that oxygen is incorporated into compound I of ch!oroperoxidase upon its formation from m-chloroperbenzoic acid (11,12). Clearly, in addition to the electron transfer processes occurring, a portion of the peroxide must be retained at the active site upon HRP-1 formation.Although many techriiques have been applied to the study of HRP compounds (I3-17), the kinetic method, in principle, provides one of the 'Author vo whom corrsspo:.dei7ce sh~a?c% be addressed better sources of informa...

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Primary compounds of catalase and peroxidase

Cited by 103 publications

References 13 publications

Spectral Properties of Bacterial Nitric-oxide Reductase

Spectral Properties of Bacterial Nitric-oxide Reductase

Proton nuclear magnetic resonance study of formate binding to metmyoglobin

Studies on Horseradish Peroxidase. XI. On the Nature of Compounds I and II as Determined from the Kinetics of the Oxidation of Ferrocyanide

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