X-ray absorption spectroscopic investigation of the resting ferrous and cosubstrate-bound active sites of phenylalanine hydroxylase

Wasinger, E. C., Mitic, N., Hedman, B., Caradonna, J., Solomon, E. I. and Hodgson, K. O. (2002) X-ray absorption spectroscopic investigation of the resting ferrous and cosubstrate-bound active sites of phenylalanine hydroxylase. Biochemistry, 41 20: 6211-6217.


Author Wasinger, E. C.
Mitic, N.
Hedman, B.
Caradonna, J.
Solomon, E. I.
Hodgson, K. O.
Title X-ray absorption spectroscopic investigation of the resting ferrous and cosubstrate-bound active sites of phenylalanine hydroxylase
Journal name Biochemistry   Check publisher's open access policy
ISSN 0006-2960
Publication date 2002
Sub-type Article (original research)
DOI 10.1021/bi0121510
Volume 41
Issue 20
Start page 6211
End page 6217
Total pages 7
Place of publication Washington
Publisher Amer Chemical Soc
Language eng
Subject 0601 Biochemistry and Cell Biology
Abstract Previous studies of ferrous wild-type phenylalanine hydroxylase, {Fe2+}PAH(T)[], have shown the active site to be a six-coordinate distorted octahedral site. After the substrate and cofactor bind to the enzyme ({Fe2+}PAH(R)[L-Phe,5-deaza-6-MPH4]), the active site converts to a five-coordinate square pyramidal structure in which the identity of the missing ligand had not been previously determined. X-ray absorption spectroscopy (XAS) at the Fe K-edge further supports this coordination number change with the binding of both cosubstrates to the enzyme, and determines this to be due to the loss of a water ligand.
Keyword Biochemistry & Molecular Biology
Amino-acid Hydroxylases
Crystal-structure
Tyrosine-hydroxylase
Substrate Activation
Electronic-structure
Circular-dichroism
Enzymatic-activity
Catalytic Domain
Iron Enzyme
Pre-edge
Q-Index Code C1
Q-Index Status Provisional Code
Institutional Status Unknown

Document type: Journal Article
Sub-type: Article (original research)
Collections: Excellence in Research Australia (ERA) - Collection
School of Chemistry and Molecular Biosciences
 
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