Degree Type

Thesis

Date of Award

2007

Degree Name

Master of Science

Department

Biochemistry, Biophysics and Molecular Biology

First Advisor

Mark Hargrove

Abstract

The x-ray crystal structure of ferric Parasponia andersonii hemoglobin has been determined to 2.3 A resolution by molecular replacement with Rice hemoglobin 1 (rHb1). By means of absorbance spectroscopy, electrochemistry and x-ray crystallography, it has been revealed that depending on the oxidation state, the heme iron can exsist in either the pentacoordinate or hexacoordinate form. Pentacoordination of the heme iron is found primarily in the deoxy ferrous (2+) form, whereas the ferric (3+) form is exhibited predominantly in bis-histidine coordination. This is unique among known forms of hemoglobins. Furthermore, the crystallographic data has provided evidence which supports previous works reporting hexacoordination of the heme iron more closely associated with the ferric state (11).

DOI

https://doi.org/10.31274/rtd-180813-16187

Publisher

Digital Repository @ Iowa State University, http://lib.dr.iastate.edu/

Copyright Owner

Andrea Savage

Language

en

Proquest ID

AAI1446051

OCLC Number

181084807

ISBN

9780549141877

File Format

application/pdf

File Size

34 pages

Share

COinS