Protein secondary-shell interactions enhance the photoinduced hydrogen production of cobalt protoporphyrin IX

作者: Dayn Joseph Sommer , Michael David Vaughn , Giovanna Ghirlanda

DOI: 10.1039/C4CC06700B

关键词:

摘要: Hydrogen is an attractive fuel with potential for production scalability, provided that inexpensive, efficient molecular catalysts utilizing base metals can be developed hydrogen production. Here we show the first time cobalt myoglobin (CoMyo) catalyzes in mild aerobic conditions turnover number of 520 over 8 hours. Compared to free Co-protoporphyrin IX, incorporation into scaffold results a 4-fold increase photoinduced activity. Engineered variants which specific histidine resides proximity active site were mutated alanine result modulation catalytic activity, H64A/H97A mutant displaying activity 2.5-fold higher than wild type. Our demonstrate protein scaffolds augment and modulate intrinsic catalysts.

参考文章(43)
Chen-zhong Li, Katsuhiko Nishiyama, Isao Taniguchi, Electrochemical and spectroelectrochemical studies on cobalt myoglobin Electrochimica Acta. ,vol. 45, pp. 2883- 2888 ,(2000) , 10.1016/S0013-4686(00)00363-7
N. S. Lewis, D. G. Nocera, Powering the planet: Chemical challenges in solar energy utilization Proceedings of the National Academy of Sciences of the United States of America. ,vol. 103, pp. 15729- 15735 ,(2006) , 10.1073/PNAS.0603395103
Philip Connolly, James H. Espenson, Cobalt-catalyzed evolution of molecular hydrogen Inorganic Chemistry. ,vol. 25, pp. 2684- 2688 ,(1986) , 10.1021/IC00236A006
Donald Bashford, David A. Case, Claudio Dalvit, Linda Tennant, Peter E. Wright, Electrostatic calculations of side-chain pKa values in myoglobin and comparison with NMR data for histidines Biochemistry. ,vol. 32, pp. 8045- 8056 ,(1993) , 10.1021/BI00082A027
Philipp Knörzer, Alexey Silakov, Carina E. Foster, Fraser A. Armstrong, Wolfgang Lubitz, Thomas Happe, Importance of the protein framework for catalytic activity of [FeFe]-hydrogenases. Journal of Biological Chemistry. ,vol. 287, pp. 1489- 1499 ,(2012) , 10.1074/JBC.M111.305797
Mark S. Hargrove, John S. Olson, The Stability of Holomyoglobin Is Determined by Heme Affinity Biochemistry. ,vol. 35, pp. 11310- 11318 ,(1996) , 10.1021/BI9603736
Jing-Xin Jian, Qiang Liu, Zhi-Jun Li, Feng Wang, Xu-Bing Li, Cheng-Bo Li, Bin Liu, Qing-Yuan Meng, Bin Chen, Ke Feng, Chen-Ho Tung, Li-Zhu Wu, None, Chitosan confinement enhances hydrogen photogeneration from a mimic of the diiron subsite of [FeFe]-hydrogenase Nature Communications. ,vol. 4, pp. 2695- ,(2013) , 10.1038/NCOMMS3695
Sonja Pullen, Honghan Fei, Andreas Orthaber, Seth M. Cohen, Sascha Ott, Enhanced Photochemical Hydrogen Production by a Molecular Diiron Catalyst Incorporated into a Metal–Organic Framework Journal of the American Chemical Society. ,vol. 135, pp. 16997- 17003 ,(2013) , 10.1021/JA407176P
Juan C. Fontecilla-Camps, Anne Volbeda, Christine Cavazza, Yvain Nicolet, Structure/function relationships of [NiFe]- and [FeFe]-hydrogenases. Chemical Reviews. ,vol. 107, pp. 4273- 4303 ,(2007) , 10.1021/CR050195Z