Anation of Lacease Type 2 Copper by Azide and Thiocyanate Ions

Robert A. Holwerda; Gary Stevens; Clinton Anderson; Max Wynn

doi:10.1021/bi00261a032

Anation of Lacease Type 2 Copper by Azide and Thiocyanate Ions

Robert A. Holwerda, Gary Stevens, Clinton Anderson, Max Wynn

Research output: Contribution to journal › Article › peer-review

11 Scopus citations

Abstract

A mechanistic study of the anation of type 2 Cu(II) in fully oxidized lacease by azide and thiocyanate ions (X^-) is reported. The rate data support a mechanism involving rapid formation of an outer-sphere complex (laccase-X^-) followed by rate-limiting dissociative interchange to give the inner-sphere complex (laccase-X-) product.

Original language	English (US)
Pages (from-to)	4403-4407
Number of pages	5
Journal	Biochemistry
Volume	21
Issue number	18
DOIs	https://doi.org/10.1021/bi00261a032
State	Published - Aug 1982

ASJC Scopus subject areas

Biochemistry

Access to Document

10.1021/bi00261a032

Cite this

@article{fc9a0653889b4a67bedec552e9d09133,

title = "Anation of Lacease Type 2 Copper by Azide and Thiocyanate Ions",

abstract = "A mechanistic study of the anation of type 2 Cu(II) in fully oxidized lacease by azide and thiocyanate ions (X-) is reported. The rate data support a mechanism involving rapid formation of an outer-sphere complex (laccase-X-) followed by rate-limiting dissociative interchange to give the inner-sphere complex (laccase-X-) product.",

author = "Holwerda, {Robert A.} and Gary Stevens and Clinton Anderson and Max Wynn",

year = "1982",

month = aug,

doi = "10.1021/bi00261a032",

language = "English (US)",

volume = "21",

pages = "4403--4407",

journal = "Biochemistry",

issn = "0006-2960",

publisher = "American Chemical Society",

number = "18",

}

TY - JOUR

T1 - Anation of Lacease Type 2 Copper by Azide and Thiocyanate Ions

AU - Holwerda, Robert A.

AU - Stevens, Gary

AU - Anderson, Clinton

AU - Wynn, Max

PY - 1982/8

Y1 - 1982/8

N2 - A mechanistic study of the anation of type 2 Cu(II) in fully oxidized lacease by azide and thiocyanate ions (X-) is reported. The rate data support a mechanism involving rapid formation of an outer-sphere complex (laccase-X-) followed by rate-limiting dissociative interchange to give the inner-sphere complex (laccase-X-) product.

AB - A mechanistic study of the anation of type 2 Cu(II) in fully oxidized lacease by azide and thiocyanate ions (X-) is reported. The rate data support a mechanism involving rapid formation of an outer-sphere complex (laccase-X-) followed by rate-limiting dissociative interchange to give the inner-sphere complex (laccase-X-) product.

UR - http://www.scopus.com/inward/record.url?scp=0020494537&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0020494537&partnerID=8YFLogxK

U2 - 10.1021/bi00261a032

DO - 10.1021/bi00261a032

M3 - Article

C2 - 7126548

AN - SCOPUS:0020494537

SN - 0006-2960

VL - 21

SP - 4403

EP - 4407

JO - Biochemistry

JF - Biochemistry

IS - 18

ER -

Anation of Lacease Type 2 Copper by Azide and Thiocyanate Ions

Abstract

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this