Sam Hart

University of York

Papers

1

Total Citations

31

H-Index

1

About

Sam Hart’s research lies at the intersection of structural biology, enzymology, and bioremediation, with a focus on the molecular mechanisms of unusual cytochrome P450 systems. His most notable contribution is the elucidation of the 1.5-Å crystal structure of XplA-heme, a unique cytochrome P450 heme domain that is C-terminally fused to its native flavodoxin redox partner. This groundbreaking work, published in 2009, revealed the structural basis for the reductive biotransformation of hexahydro-1,3,5-trinitro-1,3,5-triazine (RDX), a recalcitrant nitramine explosive and environmental pollutant. Hart’s detailed atomic-resolution model showed how XplA, in concert with the flavodoxin reductase XplB, catalyzes the breakdown of RDX, offering a promising pathway for bioremediation of contaminated sites. With 31 citations, this study remains a cornerstone in the field of explosive-degrading enzymes. Hart’s work has advanced our understanding of how nature has evolved specialized P450 systems for recalcitrant substrates, inspiring further research into enzyme engineering and environmental cleanup. His findings continue to inform efforts to harness microbial enzymes for sustainable remediation technologies.

Research Focus

Key Achievements

1
H-Index
1
Papers
31
Total Citations
31
Avg Citations/Paper
🏆 Most Cited Paper
The 1.5-Å Structure of XplA-heme, an Unusual Cytochrome P450 Heme Domain That Catalyzes Reductive Biotransformation of Royal Demolition Explosive
31 citations · 2009
📈 Most Prolific Year: 2009 (1 Papers)
🤝 Key Collaborators: 7
🏛 Institutions: University of York

Top Papers

  1. 1

Key Collaborators

Contact & Links

Available for collaboration
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