David Mulder

David Mulder

Postdoctoral Researcher

Photo of David Mulder
(303) 384-7486
At NREL Since: 

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.

Selected Publications 

  1. 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.
  2. 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.
  3. 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.
  4. 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.