PUBLICATIONS
PEER-REVIEWED ARTICLES AND REVIEWS
1. Wan, T. +, Li, S.+, Beltran, D. G.%, Schacht, A.%, Zhang, L., Becker, D. F., Zhang, L-M “Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis”, (2019) Nucleic Acids Res. (in revision).
( %undergraduate researchers)
2. Gallenito, M. J., Irvine, G., Zhang, L., Meloni, G. “Coordination plasticity guarantees metal substrate promiscuity in transmembrane primary-active Zn2+ pumps” (2019) Chem. Comm., Accepted.
3. Zhang, L. M., "X-ray absorption spectroscopy of metalloproteins", in Hu, Y. (ed.), “Metalloproteins: Methods and Protocols, Methods in Molecular Biology”, (2019), Springer Science and Business Media, Humana Press, New Jersey (invited book chapter)
4.Jiang, J+. Beltran, D.G+,%, Schacht, A.%, Zhang, L*, and Du, L*. “Functional and structural analysis of phenazine O-methyltransferase LaPhzM from Lysobacter antibioticus OH13 and one-pot enzymatic synthesis of the antibiotic myxin.” (2018) ACS Chem. Biol. 13:1003-1012
( %undergraduate researchers)
5. Li, S., Wu, X., Zhang, L., Shen, Y. and Du, L. “Activation of a cryptic gene cluster in Lysobacter enzymogenes reveals a module/domain portable mechanism of nonribosomal peptide synthetases in the biosynthesis of pyrrolopyrazines.” (2017) Org. Lett. 19: 5010-5013.
6. Spatzal, T., Schlesier, J., Burger, E. M., Sippel, D., Zhang, L., Andrade, S. L. A., Rees, D. C., Einsle, O. “Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement.” (2016) Nat. Commun.. 7: 10902-10532.
7. Anderson, J., Cutsail III, G.E., Rittle, J., Connor, B. A., Gunderson, W. A., Zhang, L.*, Hoffman, B. M.* and Peters, J. C.* “Characterization of an FeN-NH2 intermediate relevant to catalytic N2 reduction to NH3.” (2015) J Am. Chem. Soc. 137: 7803-7809.
(*corresponding authors)
8. Mattle, D., Zhang, L., Gourdon, P., Nissen, P., Rees, D. C. and Meloni, G. “A sulfur-based transport pathway for Cu+-ATPases.” (2015) EMBO J. 16: 728-740.
9. Morrison, C., Hoy, J., Zhang, L., Einsle, O. and Rees, D. C. “Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.” (2015) Biochemistry 54: 2052-2060.
10. Zhang, L., Morrison, C., Kaiser, J. T. and Rees, D. C. “Nitrogenae MoFe-protein from Clostridium pasteurianum at 1.08 Å Resolution: Comparison to the Azotobacterer vinelandii MoFe-protein.” (2015) Acta Cryst D 71: 274-282.
11.Meloni, G.+*, Zhang, L.+* and Rees, D. C.* “Transmembrane Type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.” (2014) ACS Chem. Biol. 9(1): 116-121.
12. Zhang, L., Kaiser, J. T., Meloni, G., Yang, K. Y., Spatzal, T., Andrade, S. L. A., Einsle, O., Howard, J. B. and Rees, D. C. “The sixteenth iron in the nitrogenase MoFe-protein.” (2013) Angew. Chem. Int. Ed. Engl. 52: 10529-10532.
13. Moret, M. E., Zhang, L. and Peters, J. C. “A polar copper-boron one-electron bond.” (2013) J. Am. Chem. Soc. 135: 3792-3795.
14. Pushie, J.M., Zhang, L., Pickering, I. J. and George, G. N. “The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones.” (2012) BBA - Bioenergetics. 1817: 938-947.
15. Spatzal, T., Aksoyoglu, M., Zhang, L. Andrade, S. L.A., Schleicher, E., Weber, S., Rees, D. C. and Einsle, O. “Direct evidence for interstitial carbon in nitrogenase FeMo cofactor.” (2011) Science. 334:940-940.
16. Ma, Z., Cowart, D. M., Ward, B. P., Arnold, R. J., DiMarchi, R. D., Zhang, L., George, G. N., Scott, R. A. and Giedroc, D. P. “Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor.” (2009) J. Am. Chem. Soc. 131:18044-18045.
17. Zhang, L., Lichtmanneger, J., Summer, K. H., Webb, S., Pickering, I. J. and George, G. N. “Tracing copper-thiomolybdate complexes in a prospective treatment for Wilson’s disease.” (2009) Biochemistry 48:891-897.
18. Bewer, B., Zhang, H., Zhu, Y., Zhang, L., George, G.N., Pickering, I. J. and Chapman, D. “Development of a combined K-edge subtraction and fluorescence subtraction imaging system for small animals.” (2008) Rev. Sci. Instrum. 79:085102-1-085102-3.
19. Zhang, L., Pickering, I. J., Winge, D. R. and George, G. N. “X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothionein.” (2008) Chem. Biodivers. 5:2042- 2049.
20. Zhang, H., Zhu, Y., Bewer, B., Zhang, L., Korbas, M., Pickering, I. J., George, G. N., Gupta, M. and Chapman, D. “Comparison of iodine K-edge subtraction and fluorescence subtraction imaging in an animal system.” (2008) Nucl. Instrum. Methods Phys. Res. A. 594: 283-291.
21. Chen, X., Hua, H., Balamurugan, K., Kong, X., Zhang, L., George, G. N., Georgiev, O., Schaffner, W. and Giedroc, D. P. “Copper sensing function of Drosophila metal-responsive transcription factor-1 is mediated by a tetranuclear Cu(I) cluster.” (2008) Nucleic Acids Res. 36 (9):3128-3138.
22. Zhang, L., Nelson, K. J., Rajagopalan, K.V. and George, G. N. “Structure of molybdenum center in trimethylamine N-oxide reductase from E. Coli.” (2008) Inorg. Chem. 47 (3): 1074-1078.
23. Rigby, K., Zhang, L., Cobine, P. A., Tzagoloff, A., George, G. N. and Winge, D. R. “Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae.” (2007) J. Biol. Chem. 282 (14): 10233-10244.
24. Coyne, H. J., Ciofi-Baffoni, S., Banci, L., Zhang, L., George, G. N. and Winge, D. R. “The characterization and role of zinc binding in yeast Cox4.” (2007) J. Biol. Chem. 282 (12): 8926- 8934.
25. Liu, T., Ramesh, A., Ward, S. K., Zhang, L., Ma, Z., George, G. N., Talaat, A. M., Sacchettini, J. C. and Giedroc, D. P. “CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator.” (2007) Nature Chem. Biol. 3 (1): 60-68
26. Jiang, D.T., Chen, N., Zhang, L., Malgorzata, K., Wright, G., Igarashi, R., Beauregard, D., Kirkham, M. and McKibben, M. “XAFS at Canadian Light Source.” (2007) AIP Proc. (XAFS13) 882:893-895 (conference paper).
27. Doonan, C. J., Zhang, L., Young, C. G., . “High-resolution X-ray emission spectroscopy of molybdenum compounds.” (2005) Inorg. Chem 44 (8): 2579-2581.
1. Wan, T. +, Li, S.+, Beltran, D. G.%, Schacht, A.%, Zhang, L., Becker, D. F., Zhang, L-M “Structural basis of non-canonical transcriptional regulation by the σA-bound iron-sulfur protein WhiB1 in M. tuberculosis”, (2019) Nucleic Acids Res. (in revision).
( %undergraduate researchers)
2. Gallenito, M. J., Irvine, G., Zhang, L., Meloni, G. “Coordination plasticity guarantees metal substrate promiscuity in transmembrane primary-active Zn2+ pumps” (2019) Chem. Comm., Accepted.
3. Zhang, L. M., "X-ray absorption spectroscopy of metalloproteins", in Hu, Y. (ed.), “Metalloproteins: Methods and Protocols, Methods in Molecular Biology”, (2019), Springer Science and Business Media, Humana Press, New Jersey (invited book chapter)
4.Jiang, J+. Beltran, D.G+,%, Schacht, A.%, Zhang, L*, and Du, L*. “Functional and structural analysis of phenazine O-methyltransferase LaPhzM from Lysobacter antibioticus OH13 and one-pot enzymatic synthesis of the antibiotic myxin.” (2018) ACS Chem. Biol. 13:1003-1012
( %undergraduate researchers)
5. Li, S., Wu, X., Zhang, L., Shen, Y. and Du, L. “Activation of a cryptic gene cluster in Lysobacter enzymogenes reveals a module/domain portable mechanism of nonribosomal peptide synthetases in the biosynthesis of pyrrolopyrazines.” (2017) Org. Lett. 19: 5010-5013.
6. Spatzal, T., Schlesier, J., Burger, E. M., Sippel, D., Zhang, L., Andrade, S. L. A., Rees, D. C., Einsle, O. “Nitrogenase FeMoco investigated by spatially resolved anomalous dispersion refinement.” (2016) Nat. Commun.. 7: 10902-10532.
7. Anderson, J., Cutsail III, G.E., Rittle, J., Connor, B. A., Gunderson, W. A., Zhang, L.*, Hoffman, B. M.* and Peters, J. C.* “Characterization of an FeN-NH2 intermediate relevant to catalytic N2 reduction to NH3.” (2015) J Am. Chem. Soc. 137: 7803-7809.
(*corresponding authors)
8. Mattle, D., Zhang, L., Gourdon, P., Nissen, P., Rees, D. C. and Meloni, G. “A sulfur-based transport pathway for Cu+-ATPases.” (2015) EMBO J. 16: 728-740.
9. Morrison, C., Hoy, J., Zhang, L., Einsle, O. and Rees, D. C. “Substrate pathways in the nitrogenase MoFe protein by experimental identification of small molecule binding sites.” (2015) Biochemistry 54: 2052-2060.
10. Zhang, L., Morrison, C., Kaiser, J. T. and Rees, D. C. “Nitrogenae MoFe-protein from Clostridium pasteurianum at 1.08 Å Resolution: Comparison to the Azotobacterer vinelandii MoFe-protein.” (2015) Acta Cryst D 71: 274-282.
11.Meloni, G.+*, Zhang, L.+* and Rees, D. C.* “Transmembrane Type-2-like Cu2+ site in the P1B-3-type ATPase CopB: implications for metal selectivity.” (2014) ACS Chem. Biol. 9(1): 116-121.
12. Zhang, L., Kaiser, J. T., Meloni, G., Yang, K. Y., Spatzal, T., Andrade, S. L. A., Einsle, O., Howard, J. B. and Rees, D. C. “The sixteenth iron in the nitrogenase MoFe-protein.” (2013) Angew. Chem. Int. Ed. Engl. 52: 10529-10532.
13. Moret, M. E., Zhang, L. and Peters, J. C. “A polar copper-boron one-electron bond.” (2013) J. Am. Chem. Soc. 135: 3792-3795.
14. Pushie, J.M., Zhang, L., Pickering, I. J. and George, G. N. “The fictile coordination chemistry of cuprous-thiolate sites in copper chaperones.” (2012) BBA - Bioenergetics. 1817: 938-947.
15. Spatzal, T., Aksoyoglu, M., Zhang, L. Andrade, S. L.A., Schleicher, E., Weber, S., Rees, D. C. and Einsle, O. “Direct evidence for interstitial carbon in nitrogenase FeMo cofactor.” (2011) Science. 334:940-940.
16. Ma, Z., Cowart, D. M., Ward, B. P., Arnold, R. J., DiMarchi, R. D., Zhang, L., George, G. N., Scott, R. A. and Giedroc, D. P. “Unnatural amino acid substitution as a probe of the allosteric coupling pathway in a mycobacterial Cu(I) sensor.” (2009) J. Am. Chem. Soc. 131:18044-18045.
17. Zhang, L., Lichtmanneger, J., Summer, K. H., Webb, S., Pickering, I. J. and George, G. N. “Tracing copper-thiomolybdate complexes in a prospective treatment for Wilson’s disease.” (2009) Biochemistry 48:891-897.
18. Bewer, B., Zhang, H., Zhu, Y., Zhang, L., George, G.N., Pickering, I. J. and Chapman, D. “Development of a combined K-edge subtraction and fluorescence subtraction imaging system for small animals.” (2008) Rev. Sci. Instrum. 79:085102-1-085102-3.
19. Zhang, L., Pickering, I. J., Winge, D. R. and George, G. N. “X-ray absorption spectroscopy of cuprous-thiolate clusters in Saccharomyces cerevisiae metallothionein.” (2008) Chem. Biodivers. 5:2042- 2049.
20. Zhang, H., Zhu, Y., Bewer, B., Zhang, L., Korbas, M., Pickering, I. J., George, G. N., Gupta, M. and Chapman, D. “Comparison of iodine K-edge subtraction and fluorescence subtraction imaging in an animal system.” (2008) Nucl. Instrum. Methods Phys. Res. A. 594: 283-291.
21. Chen, X., Hua, H., Balamurugan, K., Kong, X., Zhang, L., George, G. N., Georgiev, O., Schaffner, W. and Giedroc, D. P. “Copper sensing function of Drosophila metal-responsive transcription factor-1 is mediated by a tetranuclear Cu(I) cluster.” (2008) Nucleic Acids Res. 36 (9):3128-3138.
22. Zhang, L., Nelson, K. J., Rajagopalan, K.V. and George, G. N. “Structure of molybdenum center in trimethylamine N-oxide reductase from E. Coli.” (2008) Inorg. Chem. 47 (3): 1074-1078.
23. Rigby, K., Zhang, L., Cobine, P. A., Tzagoloff, A., George, G. N. and Winge, D. R. “Characterization of the cytochrome c oxidase assembly factor Cox19 of Saccharomyces cerevisiae.” (2007) J. Biol. Chem. 282 (14): 10233-10244.
24. Coyne, H. J., Ciofi-Baffoni, S., Banci, L., Zhang, L., George, G. N. and Winge, D. R. “The characterization and role of zinc binding in yeast Cox4.” (2007) J. Biol. Chem. 282 (12): 8926- 8934.
25. Liu, T., Ramesh, A., Ward, S. K., Zhang, L., Ma, Z., George, G. N., Talaat, A. M., Sacchettini, J. C. and Giedroc, D. P. “CsoR is a novel Mycobacterium tuberculosis copper-sensing transcriptional regulator.” (2007) Nature Chem. Biol. 3 (1): 60-68
26. Jiang, D.T., Chen, N., Zhang, L., Malgorzata, K., Wright, G., Igarashi, R., Beauregard, D., Kirkham, M. and McKibben, M. “XAFS at Canadian Light Source.” (2007) AIP Proc. (XAFS13) 882:893-895 (conference paper).
27. Doonan, C. J., Zhang, L., Young, C. G., . “High-resolution X-ray emission spectroscopy of molybdenum compounds.” (2005) Inorg. Chem 44 (8): 2579-2581.