Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations (2024)

Yang, T., McNaughton, R. L., Clay, M. D., Jenney, F. E., Krishnan, R., Kurtz, D. M., Adams, M. W., Johnson, M. K., & Hoffman, B. M. (2006). Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations. Journal of the American Chemical Society, 128.

Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations. / Yang, T.; McNaughton, R. L.; Clay, M. D. et al.
In: Journal of the American Chemical Society, Vol. 128, 01.01.2006.

Research output: Contribution to journal › Article › peer-review

Yang, T, McNaughton, RL, Clay, MD, Jenney, FE, Krishnan, R, Kurtz, DM, Adams, MW, Johnson, MK & Hoffman, BM 2006, 'Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations', Journal of the American Chemical Society, vol. 128.

Yang T, McNaughton RL, Clay MD, Jenney FE, Krishnan R, Kurtz DM et al. Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations. Journal of the American Chemical Society. 2006 Jan 1;128.

Yang, T. ; McNaughton, R. L. ; Clay, M. D. et al. / Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations. In: Journal of the American Chemical Society. 2006 ; Vol. 128.

@article{1e60320fc5e042f0a9d8ba64606eb341,

title = "Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations",

abstract = " Superoxide reductase (SOR) and P450 enzymes contain similar [Fe(N) 4(SCys)] active sites and, although they catalyze very different reactions, are proposed to involve analogous low-spin (hydro)peroxo-Fe(III) intermediates in their respective mechanisms that can be modeled by cyanide binding. The equatorial FeN4 ligation by four histidine ligands in CN-SOR and the heme in CN-P450cam is directly compared by 14N ENDOR, while the axial Fe-CN and Fe-S bonding is probed by 13C ENDOR of the cyanide ligand and 1H{\^I}² ENDOR measurements to determine the spin density delocalization onto the cysteine sulfur. There are small, but notable, differences in the bonding between Fe(III) and its ligands in the two enzymes. The ENDOR measurements are complemented by DFT computations that support the semiempirical equation used to compute spin densities on metal-coordinated cysteinyl and shed light on bonding changes as the Fe-C-N linkage bends. They further indicate that H bonds to the cysteinyl thiolate sulfur ligand reduce the spin density on the sulfur in both active sites to a degree that exceeds the difference induced by the alternative sets of {"}in-plane{"} nitrogen ligands. {\^A}{\textcopyright} 2006 American Chemical Society.",

author = "T. Yang and McNaughton, {R. L.} and Clay, {M. D.} and Jenney, {Francis E.} and R. Krishnan and Kurtz, {D. M.} and Adams, {Michael W.} and Johnson, {M. K.} and Hoffman, {B. M.}",

year = "2006",

month = jan,

day = "1",

language = "American English",

volume = "128",

journal = "Journal of the American Chemical Society",

}

TY - JOUR

T1 - Comparing the electronic properties of the low-spin cyano-ferric [Fe(N 4)(Cys)] active sites of superoxide reductase and P450cam using ENDOR spectroscopy and DFT calculations

AU - Yang, T.

AU - McNaughton, R. L.

AU - Clay, M. D.

AU - Jenney, Francis E.

AU - Krishnan, R.

AU - Kurtz, D. M.

AU - Adams, Michael W.

AU - Johnson, M. K.

AU - Hoffman, B. M.

PY - 2006/1/1

Y1 - 2006/1/1

N2 - Superoxide reductase (SOR) and P450 enzymes contain similar [Fe(N) 4(SCys)] active sites and, although they catalyze very different reactions, are proposed to involve analogous low-spin (hydro)peroxo-Fe(III) intermediates in their respective mechanisms that can be modeled by cyanide binding. The equatorial FeN4 ligation by four histidine ligands in CN-SOR and the heme in CN-P450cam is directly compared by 14N ENDOR, while the axial Fe-CN and Fe-S bonding is probed by 13C ENDOR of the cyanide ligand and 1Hβ ENDOR measurements to determine the spin density delocalization onto the cysteine sulfur. There are small, but notable, differences in the bonding between Fe(III) and its ligands in the two enzymes. The ENDOR measurements are complemented by DFT computations that support the semiempirical equation used to compute spin densities on metal-coordinated cysteinyl and shed light on bonding changes as the Fe-C-N linkage bends. They further indicate that H bonds to the cysteinyl thiolate sulfur ligand reduce the spin density on the sulfur in both active sites to a degree that exceeds the difference induced by the alternative sets of "in-plane" nitrogen ligands. © 2006 American Chemical Society.

AB - Superoxide reductase (SOR) and P450 enzymes contain similar [Fe(N) 4(SCys)] active sites and, although they catalyze very different reactions, are proposed to involve analogous low-spin (hydro)peroxo-Fe(III) intermediates in their respective mechanisms that can be modeled by cyanide binding. The equatorial FeN4 ligation by four histidine ligands in CN-SOR and the heme in CN-P450cam is directly compared by 14N ENDOR, while the axial Fe-CN and Fe-S bonding is probed by 13C ENDOR of the cyanide ligand and 1Hβ ENDOR measurements to determine the spin density delocalization onto the cysteine sulfur. There are small, but notable, differences in the bonding between Fe(III) and its ligands in the two enzymes. The ENDOR measurements are complemented by DFT computations that support the semiempirical equation used to compute spin densities on metal-coordinated cysteinyl and shed light on bonding changes as the Fe-C-N linkage bends. They further indicate that H bonds to the cysteinyl thiolate sulfur ligand reduce the spin density on the sulfur in both active sites to a degree that exceeds the difference induced by the alternative sets of "in-plane" nitrogen ligands. © 2006 American Chemical Society.

UR - https://digitalcommons.pcom.edu/scholarly_papers/617

M3 - Article

VL - 128

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

ER -