Papers
2
Total Citations
28
H-Index
2
About
Daniel McMullan is a structural biologist whose work has illuminated the molecular machinery of the hyperthermophilic bacterium *Thermotoga maritima*. His research focuses on the determination of three-dimensional protein structures to understand fundamental metabolic pathways. McMullan’s major contributions include solving the crystal structures of key enzymes, such as γ-glutamyl phosphate reductase (GPR), which catalyzes the second step of proline biosynthesis, and uronate isomerase, which is involved in the conversion of sugar acids. These high-resolution structures—determined at 2.0 Å and 2.85 Å, respectively—provide atomic-level insights into enzyme mechanisms and substrate binding. While his citation counts (18 and 10) reflect the specialized nature of his work, his contributions are foundational for researchers studying thermostable enzymes and microbial metabolism. McMullan’s structural studies are part of a larger, systematic effort to characterize the proteome of *T. maritima*, a model organism for understanding life at extreme temperatures. His work continues to serve as a valuable resource for enzymologists and structural biologists exploring the evolution and function of ancient metabolic pathways.
Research Focus
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Top Papers
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