Design and synthesis of multi-haem proteins. Academic Article

abstract

• 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.

authors

• Wand, Joshua

published proceedings

• Nature

altmetric score

• 3

author list (cited authors)

• Robertson, D. E., Farid, R. S., Moser, C. C., Urbauer, J. L., Mulholland, S. E., Pidikiti, R., ... Dutton, P. L.

citation count

• 538

complete list of authors

• Robertson, DE||Farid, RS||Moser, CC||Urbauer, JL||Mulholland, SE||Pidikiti, R||Lear, JD||Wand, AJ||DeGrado, WF||Dutton, PL

publication date

• March 1994

publisher

• Springer Nature  Publisher

published in

• Nature  Journal

keywords

• Amino Acid Sequence
• Drug Design
• Electrochemistry
• Electron Transport Complex III
• Hemeproteins
• Models, Molecular
• Molecular Sequence Data
• Oxidation-Reduction
• Protein Conformation
• Protein Structure, Secondary
• Spectrum Analysis

PubMed Central ID

• 8133888

Digital Object Identifier (DOI)

• 10.1038/368425a0

start page

• 425

end page

• 432

volume

• 368

issue

• 6470

URL

• http://dx.doi.org/10.1038/368425a0