Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase.

Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Research Abstract Details 

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Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Abstract Text:

K Kataoka,H Furusawa,K Takagi,K Yamaguchi,S Suzuki,

A heterologous expression system of the blue copper-containing nitrite reductase from Alcaligenes xylosoxidans GIFU1051 (AxgNIR) was constructed, and the purified recombinant enzyme was characterized. All the characteristic spectroscopic properties and enzyme activity of native AxgNIR were retained in the copper-reconstituted recombinant protein expressed in Escherichia coli, indicating the correct coordination of two types of Cu (type 1 and 2) in the recombinant enzyme. Moreover, two conserved noncoordinate residues, Asp98 and His255, located near the type 2 Cu site were replaced to elucidate the catalytic residue(s) of NIR. The Asp98 residue hydrogen-bonded to the water molecule ligating the type 2 Cu was changed to Ala, Asn, or Glu, and the His255 residue hydrogen-bonded to Asp98 through the water molecule was replaced with Ala, Lys, or Arg. The catalytic rate constants of all mutants were decreased to 0.4-2% of those of the recombinant enzyme, and the apparent K(m) values for nitrite were greatly increased in the Asp98 mutants. All the steady-state kinetic data of the mutants clearly demonstrate that both Asp98 and His255 are involved not only in the catalytic reaction but also in the substrate anchoring.

Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Publishing Authors By Initials

K Kataoka,H Furusawa,K Takagi,K Yamaguchi,S Suzuki,

For similar biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research abstracts see: biochemical phenomena, metabolism, and nutrition: biochemical phenomena: structure-activity relationship research

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Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Journal Published:

PUBLICATION TYPE: Research Support, Non-U.S. Gov

Journal: Journal of biochemistry

VOLUME: 127

Page Numbers: 345-50

Journal Abbreviation: J. Biochem.

ISSN: 0021-924X

DAY: 19

MONTH: Feb

YEAR: 2000

Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Information

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LANGUAGE: eng

NlmUniqueID: 376600

Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Keywords Mesh Terms:

KEYWORDS: Structure-Activity Relationship

MESH TERMS: metabolism

Chemical & Substance for Abstract: Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase. Information

Substance Name: Nitrite Reductases

Registry Number: EC 1.7.-

Grant and Affiliation Information for Functional analysis of conserved aspartate and histidine residues located around the type 2 copper site of copper-containing nitrite reductase.

AFFILIATION: Department of Chemistry, Graduate School of Science, Osaka University, Machikaneyama, Toyonaka, Osaka 560-0043, Japan. kataoka@ch.wani.osaka-u.ac.jp

Country: JAPAN

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MEDLINETA: J Biochem

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ACCESSION NUMBER: AB013078

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