Design and engineering of an O2 transport protein

Ronald L. Koder, J. L. Ross Anderson, Lee A. Solomon, Konda S. Reddy, Christopher C. Moser and P. Leslie Dutton ()
Additional contact information
Ronald L. Koder: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
J. L. Ross Anderson: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Lee A. Solomon: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Konda S. Reddy: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
Christopher C. Moser: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA
P. Leslie Dutton: The Johnson Research Foundation, University of Pennsylvania, Philadelphia, Pennsylvania 19104, USA

Nature, 2009, vol. 458, issue 7236, 305-309

Abstract: Abstract The principles of natural protein engineering are obscured by overlapping functions and complexity accumulated through natural selection and evolution. Completely artificial proteins offer a clean slate on which to define and test these protein engineering principles, while recreating and extending natural functions. Here we introduce this method with the design of an oxygen transport protein, akin to human neuroglobin. Beginning with a simple and unnatural helix-forming sequence with just three different amino acids, we assembled a four-helix bundle, positioned histidines to bis-histidine ligate haems, and exploited helical rotation and glutamate burial on haem binding to introduce distal histidine strain and facilitate O2 binding. For stable oxygen binding without haem oxidation, water is excluded by simple packing of the protein interior and loops that reduce helical-interface mobility. O2 affinities and exchange timescales match natural globins with distal histidines, with the remarkable exception that O2 binds tighter than CO.

Date: 2009
References: Add references at CitEc
Citations:

Downloads: (external link)
https://www.nature.com/articles/nature07841 Abstract (text/html)
Access to the full text of the articles in this series is restricted.

Related works:
This item may be available elsewhere in EconPapers: Search for items with the same title.

Export reference: BibTeX RIS (EndNote, ProCite, RefMan) HTML/Text

Persistent link: https://EconPapers.repec.org/RePEc:nat:nature:v:458:y:2009:i:7236:d:10.1038_nature07841

Ordering information: This journal article can be ordered from
https://www.nature.com/

DOI: 10.1038/nature07841

Access Statistics for this article

Nature is currently edited by Magdalena Skipper

More articles in Nature from Nature
Bibliographic data for series maintained by Sonal Shukla () and Springer Nature Abstracting and Indexing ().