The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen

Tran Chin Yang; Nathan K. Maeser; Mikhail Laryukhin; Hong In Lee; Dennis R. Dean; Lance C. Seefeldt; Brian M. Hoffman

doi:10.1021/ja0552489

The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen

Tran Chin Yang, Nathan K. Maeser, Mikhail Laryukhin, Hong In Lee, Dennis R. Dean, Lance C. Seefeldt, Brian M. Hoffman

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

77 Scopus citations

Abstract

X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe₇S₉:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either ¹⁴N or ¹⁵N as the exclusive N source. All of the ¹⁴N or ¹⁵N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N.

Original language	English
Pages (from-to)	12804-12805
Number of pages	2
Journal	Journal of the American Chemical Society
Volume	127
Issue number	37
DOIs	https://doi.org/10.1021/ja0552489
State	Published - 21 Sep 2005

Access to Document

10.1021/ja0552489

Cite this

@article{55a5167e96cd4f2686a94fb3edbb9229,

title = "The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen",

abstract = "X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe7S9:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either 14N or 15N as the exclusive N source. All of the 14N or 15N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N.",

author = "Yang, {Tran Chin} and Maeser, {Nathan K.} and Mikhail Laryukhin and Lee, {Hong In} and Dean, {Dennis R.} and Seefeldt, {Lance C.} and Hoffman, {Brian M.}",

year = "2005",

month = sep,

day = "21",

doi = "10.1021/ja0552489",

language = "English",

volume = "127",

pages = "12804--12805",

journal = "Journal of the American Chemical Society",

issn = "0002-7863",

publisher = "American Chemical Society",

number = "37",

}

TY - JOUR

T1 - The interstitial atom of the nitrogenase FeMo-cofactor

T2 - ENDOR and ESEEM evidence that it is not a nitrogen

AU - Yang, Tran Chin

AU - Maeser, Nathan K.

AU - Laryukhin, Mikhail

AU - Lee, Hong In

AU - Dean, Dennis R.

AU - Seefeldt, Lance C.

AU - Hoffman, Brian M.

PY - 2005/9/21

Y1 - 2005/9/21

N2 - X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe7S9:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either 14N or 15N as the exclusive N source. All of the 14N or 15N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N.

AB - X-ray crystallographic study of the nitrogenase MoFe protein revealed electron density from an atom (denoted X) inside the active-site metal cluster, the [MoFe7S9:homocitrate] FeMo-cofactor. The electron density associated with X is consistent with a single N, O, or C atom. We now have tested whether X is an N or not by comparing the Q-band ENDOR and ESEEM signals from resting-state (S = 3/2) MoFe protein and NMF-extracted FeMo-co from bacteria grown with either 14N or 15N as the exclusive N source. All of the 14N or 15N signals associated with the protein are lost upon extraction of the FeMo-co. We interpret this as strong evidence that X is not an N.

UR - http://www.scopus.com/inward/record.url?scp=25144493215&partnerID=8YFLogxK

U2 - 10.1021/ja0552489

DO - 10.1021/ja0552489

M3 - Article

C2 - 16159266

AN - SCOPUS:25144493215

SN - 0002-7863

VL - 127

SP - 12804

EP - 12805

JO - Journal of the American Chemical Society

JF - Journal of the American Chemical Society

IS - 37

ER -

The interstitial atom of the nitrogenase FeMo-cofactor: ENDOR and ESEEM evidence that it is not a nitrogen

Abstract

Access to Document

Other files and links

Fingerprint

Cite this