P D Barker

Bis-methionine ligation to heme iron in mutants of cytochrome b562. 1. Spectroscopic and electrochemical characterization of the electronic properties.

A J Thomson, H. Hill, A. Thomson, 1996, Biochemistry.

Coupled oxidation of heme covalently attached to cytochrome b562 yields a novel biliprotein.

I. Fearnley, P D Barker, J K Rice, 1999, Biochemistry.

Conversion of cytochrome b562 to c-type cytochromes.

S. Freund, I. Fearnley, P D Barker, 1995, Biochemistry.

Still a puzzle: why is haem covalently attached in c-type cytochromes?

S J Ferguson, S. Ferguson, P D Barker, 1999, Structure.

Transmutation of a heme protein.

R T MacGillivray, W. Funk, J. Ferrer, 1993, Proceedings of the National Academy of Sciences of the United States of America.

AGE‐RELATED CHANGES IN THE FLUORESCENCE OF MELANIN and LIPOFUSCIN GRANULES OF THE RETINAL PIGMENT EPITHELIUM: A TIME‐RESOLVED FLUORESCENCE SPECTROSCOPY STUDY

R Cubeddu, R. Ramponi, R. Cubeddu, 1991, Photochemistry and photobiology.

Bis-methionine ligation to heme iron in mutants of cytochrome b562. 2. Characterization by NMR of heme-ligand interactions.

S. Freund, P D Barker, P. Barker, 1996, Biochemistry.