Science

Current Employment:

Codexis, Bioinformatic Scientist I

Prior Employment:

2017-2020: National Renewable Energy Laboratory

Education:

2016-2017

Postdoctoral Research Fellow, Washington State University

2012-2016

Ph.D. in Biochemistry, Montana State University

2008-2012

B.S. in Biochemistry, Calvin College

Selected Publications:

10. Artz JH, , Tokmina-Lukaszewska M, Mulder DW, Lubner CE, Gutekunst K, Appel J, Bothner B, Boehm M, King PW. The structure and reactivity of the HoxEFU complex from the cyanobacterium Synechocystis sp. PCC 6803. Journal of Biological Chemistry. jbc.RA120.013136. doi:10.1074/jbc.RA120.013136

9. Artz JH, Zadvornyy OA, Mulder DW, Keable SM, Cohen AE, Ratzloff MW, Williams SG, Ginovska B, Kumar N, Song J, McPhillips SE, Davidson CM, Lyubimov AY, Pence N, Schut GJ, Jones AK, Soltis SM, Adams MWW, Raugei S, King PW, Peters JW. Tuning catalytic bias of hydrogen gas producing hydrogenases. Journal of the American Chemical Society 142 (3), 1227-1235

8. Ratzloff MW, Artz JH, Mulder DW, Collins RT, Furtak TE, King PW. (2018) CO-bridged H-Cluster intermediates in the catalytic mechanism of [FeFe]-hydrogenase CaI. Journal of the American Chemical Society. doi: 10.1021/jacs.8b03072

7. Artz JH, Mulder DW, Poudel S, Colman D, Schut GJ, Williams, SG, Jones AK, Adams MWW, Boyd ES, King PW, Peters JW. (2018) Structure-Function of [FeFe]- and [NiFe]- Hydrogenases: An Overview of Diversity, Mechanism, Maturation, and Bifurcation. Royal Society of Chemistry.

6. Artz JH, Zadvornyy OA, Mulder DW, King PW, Peters JW. (2017) Structural Characterization of Poised States in the Oxygen Sensitive Hydrogenases and Nitrogenases. Methods in enzymology 595, 213-259

5. Ledbetter RN, Garcia Costas AM, Lubner CE, Mulder DW, Tokmina-Lukaszewska M, Artz JH, Patterson A, Magnuson TS, Jay ZJ, Duan HD, Miller J, Plunkett MH, Hoben JP, Barney BM, Carlson RP, Miller AF, Bothner B, King PW, Peters JW, Seefeldt LC. (2017) The electron bifurcating FixABCX protein complex from Azotobacter vinelandii: generation of low-potential reducing equivalents for nitrogenase catalysis. Biochemistry. doi: 10.1021/acs.biochem.7b00389

4. Therien JB, Artz JH, Poudel S, Hamilton TL, Liu Z, Noone SM, Adams MWW, King PW, Bryant DA, Boyd ES, Peters JW. (2017) The physiological functions and structural determinants of catalytic bias in the [FeFe]-hydrogenases CpI and CpII of Clostridium pasteurianum strain W5. Frontiers in Microbiology. doi: 10.3389/fmicb.2017.01305

3. Artz JH, Mulder DW, Ratzloff MW, Lubner CE, Zadvornyy OA, LeVan AX, Williams SG, Adams MWW, Jones AK, King PW, Peters JW. (2017) The reduction potentials of [FeFe]-hydrogenase accessory iron-sulfur clusters provide insights into the energetics of proton reduction catalysis. J Am Chem Soc. doi: 10.1021/jacs.7b02099.

2. Artz JH, White SN, Zadvornyy OA, Fugate CJ, Hicks D, Gauss GH, Posewitz MC, Boyd ES, Peters JW. (2015) Biochemical and Structural Properties of a Thermostable Mercuric Ion Reductase from Metallosphaera sedula. Front Bioeng Biotechnol. Jul 13;3:97. doi: 10.3389/fbioe.2015.00097. eCollection 2015. PubMed PMID: 26217660; PubMed Central PMCID: PMC4500099.

1. Swanson KD, Ratzloff MW, Mulder DW, Artz JH, Ghose S, Hoffman A, White S, Zadvornyy OA, Broderick JB, Bothner B, King PW, Peters JW. (2015) [FeFe]- hydrogenase oxygen inactivation is initiated at the H cluster 2Fe subcluster. J Am Chem Soc. Feb 11;137(5):1809-16. doi: 10.1021/ja510169s. Epub 2015 Jan 29. PubMed PMID: 25579778.