David Mulder completed his Ph.D. in Biochemistry in 2010 from Montana State University after receiving a B.S. in Chemistry at Calvin College in 2005. At Montana State under Professor John Peters, his research revolved around structure-function studies of metalloenzymes, specifically investigating the maturation of [FeFe]-hydrogenases.
Dr. Mulder's main thesis work involved utilizing a wide array of biophysical techniques and x-ray crystallography to characterize an intermediate form of green algae hydrogenase, which shed light on the mechanism of [FeFe]-hydrogenase activation along with basic principles as to how complex metal clusters in general assemble in nature. At NREL, his current research includes developing a high-throughput screen with the goal of identifying oxygen-tolerant bacterial hydrogenases. These studies use ongoing structural studies as an approach to identify basic and specific properties of hydrogenases vital toward improving the enzyme's overall tolerance to oxygen.
- Mulder, DW; Boyd, ES; Sarma, R; Lange, RK; Endrizzi, JA; Broderick, JB; Peters, JW. (2010). "Stepwise [FeFe]-hydrogenase H-cluster assembly revealed in the structure of HydA(DeltaEFG)." Nature (465); pp. 248-251.
- Pandey, AS; Mulder, DW; Ensign, AS; Peters, JW. (2011). "Structural basis for carbon dioxide binding by 2-ketopropyl coenzyme M oxidoreductase/carboxylase." FEBS Lett. (585); pp. 459-464.
- Mulder, DW; Ortillo, DO; Gardenghi, DJ; Naumov, AV; Ruebush, SS; Szilagyi, RK; Huynh B; Broderick, JB; Peters, JW. (2009). "Activation of HydA(DeltaEFG) requires a preformed [4Fe-4S] cluster." Biochemistry (48); pp. 6240-6248.
- Sarma R; Mulder, DW; Brecht, E; Szilagy, RK; Seefeldt, LC; Tsuruta, H; Peters, JW. (2007). "Probing the MgATP-bound conformation of the nitrogenase Fe protein by solution small-angle X-ray scattering." Biochemistry (46); pp. 14058-14066.