Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO

Feng Chun Lo, Chang Chih Hsieh, Manuel Maestre-Reyna, Chin Yu Chen, Tzu Ping Ko, Yih Chern Horng, Yei Chen Lai, Yun Wei Chiang, Chih Mao Chou, Cheng Hung Chiang, Wei Ning Huang, Yi Hung Lin, D. Scott Bohle, Wen Feng Liaw

Research output: Contribution to journalArticle

9 Citations (Scopus)

Abstract

Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and17O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII–FeIIIdiiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII–FeIIYtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress.

Original languageEnglish
Pages (from-to)9768-9776
Number of pages9
JournalChemistry - A European Journal
Volume22
Issue number28
DOIs
Publication statusPublished - 2016 Jan 1

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Repair
Iron
Crystal structure
Proteins
Nitric oxide
Dichroism
Histidine
Structural analysis
Labeling
Paramagnetic resonance
Tunnels
Nitric Oxide
Modulation
Fluxes
X rays
Electrons
Substrates

All Science Journal Classification (ASJC) codes

  • Catalysis
  • Organic Chemistry

Cite this

Lo, Feng Chun ; Hsieh, Chang Chih ; Maestre-Reyna, Manuel ; Chen, Chin Yu ; Ko, Tzu Ping ; Horng, Yih Chern ; Lai, Yei Chen ; Chiang, Yun Wei ; Chou, Chih Mao ; Chiang, Cheng Hung ; Huang, Wei Ning ; Lin, Yi Hung ; Bohle, D. Scott ; Liaw, Wen Feng. / Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO. In: Chemistry - A European Journal. 2016 ; Vol. 22, No. 28. pp. 9768-9776.
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abstract = "Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and17O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII–FeIIIdiiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII–FeIIYtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress.",
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Lo, FC, Hsieh, CC, Maestre-Reyna, M, Chen, CY, Ko, TP, Horng, YC, Lai, YC, Chiang, YW, Chou, CM, Chiang, CH, Huang, WN, Lin, YH, Bohle, DS & Liaw, WF 2016, 'Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO', Chemistry - A European Journal, vol. 22, no. 28, pp. 9768-9776. https://doi.org/10.1002/chem.201600990

Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO. / Lo, Feng Chun; Hsieh, Chang Chih; Maestre-Reyna, Manuel; Chen, Chin Yu; Ko, Tzu Ping; Horng, Yih Chern; Lai, Yei Chen; Chiang, Yun Wei; Chou, Chih Mao; Chiang, Cheng Hung; Huang, Wei Ning; Lin, Yi Hung; Bohle, D. Scott; Liaw, Wen Feng.

In: Chemistry - A European Journal, Vol. 22, No. 28, 01.01.2016, p. 9768-9776.

Research output: Contribution to journalArticle

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T1 - Crystal Structure Analysis of the Repair of Iron Centers Protein YtfE and Its Interaction with NO

AU - Lo, Feng Chun

AU - Hsieh, Chang Chih

AU - Maestre-Reyna, Manuel

AU - Chen, Chin Yu

AU - Ko, Tzu Ping

AU - Horng, Yih Chern

AU - Lai, Yei Chen

AU - Chiang, Yun Wei

AU - Chou, Chih Mao

AU - Chiang, Cheng Hung

AU - Huang, Wei Ning

AU - Lin, Yi Hung

AU - Bohle, D. Scott

AU - Liaw, Wen Feng

PY - 2016/1/1

Y1 - 2016/1/1

N2 - Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and17O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII–FeIIIdiiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII–FeIIYtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress.

AB - Molecular mechanisms underlying the repair of nitrosylated [Fe–S] clusters by the microbial protein YtfE remain poorly understood. The X-ray crystal structure of YtfE, in combination with EPR, magnetic circular dichroism (MCD), UV, and17O-labeling electron spin echo envelope modulation measurements, show that each iron of the oxo-bridged FeII–FeIIIdiiron core is coordinatively unsaturated with each iron bound to two bridging carboxylates and two terminal histidines in addition to an oxo-bridge. Structural analysis reveals that there are two solvent-accessible tunnels, both of which converge to the diiron center and are critical for capturing substrates. The reactivity of the reduced-form FeII–FeIIYtfE toward nitric oxide demonstrates that the prerequisite for N2O production requires the two iron sites to be nitrosylated simultaneously. Specifically, the nitrosylation of the two iron sites prior to their reductive coupling to produce N2O is cooperative. This result suggests that, in addition to any repair of iron centers (RIC) activity, YtfE acts as an NO-trapping scavenger to promote the NO to N2O transformation under low NO flux, which precedes nitrosative stress.

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