Matthew
H. Sazinsky |
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Peer Reviewed Publications
UNDERGRADUATE AUTHORS ARE UNDERLINED
Sazinsky,
M. H, LeMoine, B., Orofino, M.,
Davydov, R., Bencze, K., Mandal, A. K., Stemmler, T. L., Hoffman, B. M.,
Argüello, J. M., Rosenzweig, A. C. Characterization and Structure of
a Novel Zn2+ and [2Fe-2S]-Containing Copper Chaperone from Archaeoglobus
fulgidus. J. Biol. Chem. 2007, 282, 25950-25959.
Sazinsky,
M. H., Dunten, P., McCormick, M.
S., Di Donato, A., Lippard, S. J. X-ray Structure of a Hydroxylase-Effector
Protein Complex from a Hydrocarbon Oxidizing Multicomponent Monoxygenase. Biochemistry. 2006,
45, 15392-15404.
Rosenzweig,
A. C. Sazinsky, M. H. Structural
insights into dioxygen-activating copper enzymes. Curr. Opin. Struct. Biol. 2006,
16, 729-735.
McCormick,
M. S., Sazinsky, M. H., Condon
K. L., Lippard, S. J. X-ray Structure of Manganese(II) Reconstituted
Toluene /o-Xylene Monooxygenase Hydroxylase, J. Am. Chem. Soc. 2006,
128, 15108-15110.
Sazinsky,
M. H., Lippard, S. J. Correlating
Structure with Function in Bacterial Multicomponent Monooxygenases and Related
Diiron Proteins. Acc. Chem.
Res. 2006, 39,
556-566.
Sazinsky,
M. H., Agarwal, S., Argüello, J.
M., Rosenzweig A. C., Structure of the Actuator Domain from the Archaeoglobus
fulgidus Cu+-ATPase. Biochemistry. 2006,
45, 9949-9955.
Sazinsky,
M. H., Mandal, A. K., Argüello, J.
M., Rosenzweig, A. C. Structure and Characterization of the ATP Binding Domain
from the Archaeoglobus fulgidus
Copper Transporting P1-Type ATPase CopA. J. Biol. Chem. 2006,
281, 11161-11166.
Jackson
Rudd, D. Sazinsky, M. H., Lippard,
S. J., Hedman, B., Hodgson, K. O. X-ray Absorption Spectroscopic Study of the
Reduced Hydroxylases of Methane Monooxygenase and Toluene/o-Xylene
Monooxygenase: Differences in
Active Site Structure and Effects of the Coupling Proteins MMOB and ToMOD. Inorg.
Chem., 2005, 44,
4546-4554.
Lu,
S., Sazinsky, M. H., Whittaker,
J. W., Lippard, S. J.; Moenne-Loccoz, P. Fourier Transform Infrared
Characterization of the Azido Complex of Methane Monooxygenase Hydroxylase from
Methylococcus capsulatus (Bath).
J. Am. Chem. Soc., 2005, 127,
4148-4149.
Sazinsky, M. H., Lippard, S. J. Product Bound Structures of the Soluble Methane
Monooxygenase Hydroxylase from Methylococcus capsulatus (Bath): Protein Motion in the a-Subunit. J.
Am. Chem. Soc., 2005, 127,
5814-5825.
Sazinsky, M. H., Merkx, M., Tang, S., Lippard, S. J. Coordination Chemistry at an Enzyme Active Site; Preparation
and X-ray Structures of Metal-free, Dicobalt and Dimanganese Forms of Soluble
Methane Monooxygenase Hydroxylase. Biochemistry. 2005,
43, 4579-4589
Jackson-Rudd, D., Sazinsky, M. H., Merkx, M., Lippard, S. J., Hedman, B., Hodgson, K.
O. Determination by X-ray
Absorption Spectroscopy of the Fe-Fe Separation in the Oxidized Form of the
Hydroxylase of Methane Monooxygenase Alone and in the Presence of MMOD. Inorg.
Chem. 2004, 43,
4579-4589.
Sazinsky, M. H., Bard, J., DiDonato, A., Lippard, S. J. Crystal Structure of the
Toluene/ o-Xylene Monooxygenase
Hydroxylase from Pseudomonas stutzeri OX1: Insight into the
Substrate Specificity, Substrate Channeling and Active Site Tuning of
Multicomponent Monooxygenases J. Biol. Chem. 2004,
279, 10600-10610.
MacArthur, R., Sazinsky, M. H., Kuhne, H., Whittington, D. A., Lippard, S. J.,
Brudvig, G. Component B Binding to
the Soluble Methane Monooxygenase Hydroxylase by Saturation-Recovery EPR
Spectroscopy of Spin-Labeled MMOB. J. Am. Chem. Soc.
2002, 124, 13392-13393.
Merkx, M. Kopp, D. A., Sazinsky, M. H., Muller, J., Blazyk, J. B., Lippard, S. J. Dioxygen
Activation and Methane Hydroxylation by Soluble Methane Monooxygenase: A Tale of Two Irons and Three
Proteins. Angew Chem. Int.
Edit. 2001, 40,
2782-2807.
Whittington, D. A., Sazinsky, M. H., and Lippard, S. J. X-ray Crystal Structure of Alcohol Products Bound at the
Active Site of Soluble Methane Monooxygenase Hydroxylase. J. Am. Chem. Soc. 2001,
123, 1794-1795.
Jaffe, E. K., Volin, M., Bronson-Mullins, C. R.,
Dunbrack, D. L., Kervinen, J., Martins, J., Quinlan, J. F., Sazinsky, M. H., Steinhouse, E. M., Yeung, A. T. An Artificial Gene for Human
Porphobilinogen Synthase Allows Comparison of an Allelic Variation Implicated
in Susceptibility to Lead Poisoning.
J. Biol. Chem. 2000, 275,
2619-2626.