Design and synthesis of multi-haem proteins.
A water-soluble, 62-residue, di-alpha-helical peptide has been synthesized which accommodates two bis-histidyl haem groups. The peptide assembles into a four-helix dimer with 2-fold symmetry and four parallel haems that closely resemble native haems in their spectral and electrochemical properties, including haem-haem redox interaction. This protein is an essential intermediate in the synthesis of molecular 'maquettes', a novel class of simplified versions of the metalloproteins involved in redox catalysis and in energy conversion in respiratory and photosynthetic electron transfer.
Robertson
D E
DE
Johnson Research Foundation, Department of Biochemistry and Biophysics, University of Pennsylvania, Philadelphia 19104.
Farid
R S
RS
Moser
C C
CC
Urbauer
J L
JL
Mulholland
S E
SE
Pidikiti
R
R
Lear
J D
JD
Wand
A J
AJ
DeGrado
W F
WF
Dutton
P L
PL
D000595:Amino Acid Sequence; D015195:Drug Design; D004563:Electrochemistry; D014450:Electron Transport Complex III / Q000138:chemical synthesis / Q000737:chemistry; D006420:Hemeproteins / Q000138:chemical synthesis* / Q000737:chemistry; D008958:Models, Molecular; D008969:Molecular Sequence Data; D010084:Oxidation-Reduction; D011487:Protein Conformation; D017433:Protein Structure, Secondary; D013057:Spectrum Analysis
D006420:Hemeproteins; D014450:Electron Transport Complex III