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Reversible dioxygen binding in solvent-free liquid myoglobin

DOI: 10.1038/nchem.700 DOI Help

Authors: Adam W. Perriman (University of Bristol) , Alex P. S. Brogan (University of Bristol) , Helmut Cölfen (Max-Planck-Institute of Colloids and Interfaces) , Nikolaos Tsoureas (University of Bristol) , Gareth R. Owen (University of Bristol) , Stephen Mann (University of Bristol)
Co-authored by industrial partner: No

Type: Journal Paper
Journal: Nature Chemistry , VOL 2 (8) , PAGES 622 - 626

State: Published (Approved)
Published: June 2010

Abstract: The ensemble of forces that stabilize protein structure and facilitate biological function are intimately linked with the ubiquitous aqueous environment of living systems. As a consequence, biomolecular activity is highly sensitive to the interplay of solvent-protein interactions, and deviation from the native conditions, for example by exposure to increased thermal energy or severe dehydration, results in denaturation and subsequent loss of function. Although certain enzymes can be extracted into non-aqueous solvents without significant loss of activity, there are no known examples of solvent-less (molten) liquids of functional metalloproteins. Here we describe the synthesis and properties of room-temperature solvent-free myoglobin liquids with near-native structure and reversible dioxygen binding ability equivalent to the haem protein under physiological conditions. The realization of room-temperature solvent-free myoglobin liquids with retained function presents novel challenges to existing theories on the role of solvent molecules in structural biology, and should offer new opportunities in protein-based nanoscience and bionanotechnology.

Subject Areas: Chemistry, Biology and Bio-materials

Instruments: B23-Circular Dichroism

Added On: 26/09/2012 12:10

Discipline Tags:

Biochemistry Chemistry Life Sciences & Biotech

Technical Tags:

Spectroscopy Circular Dichroism (CD)