Paramagnetic 13C and 13N NMR analyses of cyanide- (13C13N-) ligated ferric peroxidases

The push effect, not pull effect, modulates the compound formation rate

Daisuke Nonaka, Hiroyuki Wariishi, Hiroshi Fujii

Research output: Contribution to journalArticle

12 Citations (Scopus)

Abstract

Paramagnetic 13C and 15N NMR spectroscopy of heme-bound cyanide (13C15N) was utilized to quantitatively distinguish the electron donor effect (the push effect) from the proximal histidine and hydrogen-bonding effect (the pull effect) from the distal amino acid residues in cytochrome c peroxidase (CcP), ascorbate peroxidase (APX), lignin peroxidase (LiP), and manganese peroxidase (MnP). Paramagnetic 13C NMR signals of heme-bound 13C15N of these peroxidases were observed in a wide range, -3501 ppm (CcP), -3563 ppm (APX), -3823 ppm (MnP), and -3826 ppm (LiP), while paramagnetic 15N NMR signals of those were detected in a narrow range, 574 ppm (ARP), 605 ppm (CcP), 626 ppm (LiP), and 654 ppm (MnP). Detailed analysis, combined with the previous results for horseradish peroxidase and Arthromyces ramosus peroxidase, indicated that the push effect is quite different among these peroxidases while the pull effect is similar. More importantly, a strong correlation between the 13C NMR shift (the push effect) and the compound I formation rate was observed, indicating that the push effect causes a variation in the compound I formation rate. Comparison of the 13C and 15N NMR results of these peroxidases with their crystal structures suggests that the orientation of the proximal imidazole plane to the heme N - Fe - N axis controls the push effect and the compound I formation rate of peroxidase.

Original languageEnglish
Pages (from-to)898-905
Number of pages8
JournalBiochemistry
Volume48
Issue number5
DOIs
Publication statusPublished - Feb 10 2009

Fingerprint

manganese peroxidase
Peroxidases
Cytochrome-c Peroxidase
Cyanides
Heme
Nuclear magnetic resonance
Ascorbate Peroxidases
Peroxidase
Horseradish Peroxidase
Hydrogen Bonding
Histidine
Crystal orientation
Nuclear magnetic resonance spectroscopy
Hydrogen bonds
Magnetic Resonance Spectroscopy
Crystal structure
Electrons
Amino Acids
Carbon-13 Magnetic Resonance Spectroscopy
lignin peroxidase

All Science Journal Classification (ASJC) codes

  • Biochemistry

Cite this

Paramagnetic 13C and 13N NMR analyses of cyanide- (13C13N-) ligated ferric peroxidases : The push effect, not pull effect, modulates the compound formation rate. / Nonaka, Daisuke; Wariishi, Hiroyuki; Fujii, Hiroshi.

In: Biochemistry, Vol. 48, No. 5, 10.02.2009, p. 898-905.

Research output: Contribution to journalArticle

@article{9081af6223fb40a9884eea477dd752fa,
title = "Paramagnetic 13C and 13N NMR analyses of cyanide- (13C13N-) ligated ferric peroxidases: The push effect, not pull effect, modulates the compound formation rate",
abstract = "Paramagnetic 13C and 15N NMR spectroscopy of heme-bound cyanide (13C15N) was utilized to quantitatively distinguish the electron donor effect (the push effect) from the proximal histidine and hydrogen-bonding effect (the pull effect) from the distal amino acid residues in cytochrome c peroxidase (CcP), ascorbate peroxidase (APX), lignin peroxidase (LiP), and manganese peroxidase (MnP). Paramagnetic 13C NMR signals of heme-bound 13C15N of these peroxidases were observed in a wide range, -3501 ppm (CcP), -3563 ppm (APX), -3823 ppm (MnP), and -3826 ppm (LiP), while paramagnetic 15N NMR signals of those were detected in a narrow range, 574 ppm (ARP), 605 ppm (CcP), 626 ppm (LiP), and 654 ppm (MnP). Detailed analysis, combined with the previous results for horseradish peroxidase and Arthromyces ramosus peroxidase, indicated that the push effect is quite different among these peroxidases while the pull effect is similar. More importantly, a strong correlation between the 13C NMR shift (the push effect) and the compound I formation rate was observed, indicating that the push effect causes a variation in the compound I formation rate. Comparison of the 13C and 15N NMR results of these peroxidases with their crystal structures suggests that the orientation of the proximal imidazole plane to the heme N - Fe - N axis controls the push effect and the compound I formation rate of peroxidase.",
author = "Daisuke Nonaka and Hiroyuki Wariishi and Hiroshi Fujii",
year = "2009",
month = "2",
day = "10",
doi = "10.1021/bi802030a",
language = "English",
volume = "48",
pages = "898--905",
journal = "Biochemistry",
issn = "0006-2960",
publisher = "American Chemical Society",
number = "5",

}

TY - JOUR

T1 - Paramagnetic 13C and 13N NMR analyses of cyanide- (13C13N-) ligated ferric peroxidases

T2 - The push effect, not pull effect, modulates the compound formation rate

AU - Nonaka, Daisuke

AU - Wariishi, Hiroyuki

AU - Fujii, Hiroshi

PY - 2009/2/10

Y1 - 2009/2/10

N2 - Paramagnetic 13C and 15N NMR spectroscopy of heme-bound cyanide (13C15N) was utilized to quantitatively distinguish the electron donor effect (the push effect) from the proximal histidine and hydrogen-bonding effect (the pull effect) from the distal amino acid residues in cytochrome c peroxidase (CcP), ascorbate peroxidase (APX), lignin peroxidase (LiP), and manganese peroxidase (MnP). Paramagnetic 13C NMR signals of heme-bound 13C15N of these peroxidases were observed in a wide range, -3501 ppm (CcP), -3563 ppm (APX), -3823 ppm (MnP), and -3826 ppm (LiP), while paramagnetic 15N NMR signals of those were detected in a narrow range, 574 ppm (ARP), 605 ppm (CcP), 626 ppm (LiP), and 654 ppm (MnP). Detailed analysis, combined with the previous results for horseradish peroxidase and Arthromyces ramosus peroxidase, indicated that the push effect is quite different among these peroxidases while the pull effect is similar. More importantly, a strong correlation between the 13C NMR shift (the push effect) and the compound I formation rate was observed, indicating that the push effect causes a variation in the compound I formation rate. Comparison of the 13C and 15N NMR results of these peroxidases with their crystal structures suggests that the orientation of the proximal imidazole plane to the heme N - Fe - N axis controls the push effect and the compound I formation rate of peroxidase.

AB - Paramagnetic 13C and 15N NMR spectroscopy of heme-bound cyanide (13C15N) was utilized to quantitatively distinguish the electron donor effect (the push effect) from the proximal histidine and hydrogen-bonding effect (the pull effect) from the distal amino acid residues in cytochrome c peroxidase (CcP), ascorbate peroxidase (APX), lignin peroxidase (LiP), and manganese peroxidase (MnP). Paramagnetic 13C NMR signals of heme-bound 13C15N of these peroxidases were observed in a wide range, -3501 ppm (CcP), -3563 ppm (APX), -3823 ppm (MnP), and -3826 ppm (LiP), while paramagnetic 15N NMR signals of those were detected in a narrow range, 574 ppm (ARP), 605 ppm (CcP), 626 ppm (LiP), and 654 ppm (MnP). Detailed analysis, combined with the previous results for horseradish peroxidase and Arthromyces ramosus peroxidase, indicated that the push effect is quite different among these peroxidases while the pull effect is similar. More importantly, a strong correlation between the 13C NMR shift (the push effect) and the compound I formation rate was observed, indicating that the push effect causes a variation in the compound I formation rate. Comparison of the 13C and 15N NMR results of these peroxidases with their crystal structures suggests that the orientation of the proximal imidazole plane to the heme N - Fe - N axis controls the push effect and the compound I formation rate of peroxidase.

UR - http://www.scopus.com/inward/record.url?scp=61449094886&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=61449094886&partnerID=8YFLogxK

U2 - 10.1021/bi802030a

DO - 10.1021/bi802030a

M3 - Article

VL - 48

SP - 898

EP - 905

JO - Biochemistry

JF - Biochemistry

SN - 0006-2960

IS - 5

ER -