Binding mode of benzhydroxamic acid to <i>Arthromyces ramosus</i> peroxidase shown by X‐ray crystallographic analysis of the complex at 1.6 Å resolution

Itakura, Hikaru; Oda, Yutaka; Fukuyama, Keiichi

doi:10.1016/s0014-5793(97)00751-5

Cited by 69 publications

(64 citation statements)

References 28 publications

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“…Computational analyses of the mtCP structure identified an energetically favorable binding site for INH near the ␦-meso edge of the heme (2). This location is similar to that observed for other small aromatic compounds in the crystal structures of class I, II, and III peroxidases (13)(14)(15)(16)). An alternative binding site has also been suggested based upon crystallographic studies of the Burkholderia pseudomallei CP, which places INH in a surface loop structure (17) ϳ10 Å away from the binding site of small aromatic compounds located near the ␦-meso edge of the heme.…”

supporting

confidence: 67%

“…8A (8). Using 14 N, 15 N or 15 N, 14 N isomers of INH, singly labeled at the hydrazide moiety, the level of incorporation of label into the amide end product was determined using HPLC and electrospray mass spectrometry methods. In the case of mtCP, the amide reaction product obtained con- (panels A-C).…”

Section: Resultsmentioning

confidence: 99%

“…Reactions were carried out in 50 mM Na 2 HPO 4 , pH 7. 14 N isomers of INH, and 10 M H 2 O 2 in a total volume of 1 ml. Reactions were incubated overnight at 37°C.…”

Section: Methodsmentioning

confidence: 99%

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Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Pierattelli

Banci

Eady

et al. 2004

Journal of Biological Chemistry

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There is an urgent need to understand the mechanism of activation of the frontline anti-tuberculosis drug isoniazid by the Mycobacterium tuberculosis catalase-peroxidase. To address this, a combination of NMR spectroscopic, biochemical, and computational methods have been used to obtain a model of the frontline anti-tuberculosis drug isoniazid bound to the active site of the class III peroxidase, horseradish peroxidase C. This information has been used in combination with the new crystal structure of the M. tuberculosis catalase-peroxidase to predict the mode of INH binding across the class I heme peroxidase family. An enzyme-catalyzed mechanism for INH activation is proposed that brings together structural, functional, and spectroscopic data from a variety of sources. Collectively, the information not only provides a molecular basis for understanding INH activation by the M. tuberculosis catalase-peroxidase but also establishes a new conceptual framework for testing hypotheses regarding the enzyme-catalyzed turnover of this compound in a number of heme peroxidases.

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supporting

confidence: 67%

Section: Resultsmentioning

confidence: 99%

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Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Pierattelli

Banci

Eady

et al. 2004

Journal of Biological Chemistry

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“…The CHB in the -meso carbon and ferryl oxygen por (•+) cation radical is of [-7.66 --7.69eV] which is considered to be electron donor as HOMO nucleophilic Sr (0.860, 0.766). It should give the intermolecular space to the possible ET mechanism of peroxidase reaction that distance between the -NH-OH oxygen atoms of SHA and the nitrogen atom of cyanide heme Fe is shorter than those the ferryl oxygen atom of Fe IV =O of CCP (Itakura et al,1997) .…”

Section: [R409l] Structure Based Molecular Orbital Study With Oda and Cnmentioning

confidence: 99%

Functional Implication Guided by Structure-Based Study on Catalase – Peroxidase (KatG) from Haloarcula Marismortui

Sato¹

2012

Chemical Biology

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“…Benzhydroxamic acid (BHA) is known to form kinetically tight complexes with most peroxidases, in particular with HRP isozyme C (19). The crystallographic analyses of ARP-BHA complex (20) and HRP isozyme C-BHA complex (21) showed unequivocally how BHA binds to the distal pocket in both enzymes. The hydrophilic portion of BHA forms hydrogen bonds to the distal catalytic His and Arg and to backbone oxygen of Pro in ARP.…”

mentioning

confidence: 95%

Direct Binding of Hydroxylamine to the Heme Iron ofArthromyces ramosus Peroxidase

Wariishi¹,

Nonaka²,

Johjima³

et al. 2000

Journal of Biological Chemistry

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The interaction of hydroxylamine (HA) with Arthromyces ramosus peroxidase (ARP) was investigated by kinetic, spectroscopic, and x-ray crystallographic techniques. HA inhibited the reaction of native ARP with H 2 O 2 in a competitive manner. Electron absorption and resonance Raman spectroscopic studies indicated that pentacoordinate high spin species of native ARP are converted to hexacoordinate low spin species upon the addition of HA, strongly suggesting the occurrence of a direct interaction of HA with ARP heme iron. Kinetic analysis exhibited that the apparent dissociation constant is 6.2 mM at pH 7.0 and that only one HA molecule likely binds to the vicinity of the heme. pH dependence of HA binding suggested that the nitrogen atom of HA could be involved in the interaction with the heme iron. X-ray crystallographic analysis of ARP in complex with HA at 2.0 Å resolution revealed that the electron density ascribed to HA is located in the distal pocket between the heme iron and the distal His 56 . HA seems to directly interact with the heme iron but is too far away to interact with Arg 52

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Binding mode of benzhydroxamic acid to Arthromyces ramosus peroxidase shown by X‐ray crystallographic analysis of the complex at 1.6 Å resolution

Cited by 69 publications

References 28 publications

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Enzyme-catalyzed Mechanism of Isoniazid Activation in Class I and Class III Peroxidases

Functional Implication Guided by Structure-Based Study on Catalase – Peroxidase (KatG) from Haloarcula Marismortui

Direct Binding of Hydroxylamine to the Heme Iron ofArthromyces ramosus Peroxidase

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