In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase
Само за регистроване кориснике
2011
Аутори
Farquhar, Erik R.Emerson, Joseph P.
Koehntop, Kevin D.
Reynolds, Mark F.
Trmčić, Milena
Que, Jr., Lawrence
Чланак у часопису (Објављена верзија)
Метаподаци
Приказ свих података о документуАпстракт
The homoprotocatechuate 2,3-dioxygenase from Arthrobacter globiformis (MndD) catalyzes the oxidative ring cleavage reaction of its catechol substrate in an extradiol fashion. Although this reactivity is more typically associated with non-heme iron enzymes, MndD exhibits an unusual specificity for manganese(II). MndD is structurally very similar to the iron(II)-dependent homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum (HPCD), and we have previously shown that both MndD and HPCD are equally active towards substrate turnover with either iron(II) or manganese(11) (Emerson et al. in Proc. Natl. Acad. Sci. USA 105:7347-7352, 2008). However, expression of MndD in Escherichia coli under aerobic conditions in the presence of excess iron results in the isolation of inactive blue-green iron-substituted MndD. Spectroscopic studies indicate that this form of iron-substituted MndD contains an iron(III) center with abound catecholate, which is presumably generated by in vivo self-hydro...xylation of a second-sphere tyrosine residue, as found for other self-hydroxylated non-heme iron oxygenases. The absence of this modification in either the native manganese-containing MndD or iron-containing HPCD suggests that the metal center of iron-substituted MndD is able to bind and activate 02 in the absence of its substrate, employing a high-valence oxoiron oxidant to carry out the observed self-hydroxylation chemistry. These results demonstrate that the active site metal in MndD can support two dramatically different 02 activation pathways, further highlighting the catalytic flexibility of enzymes containing a 2-His-1-carboxylate facial triad metal binding motif.
Кључне речи:
2-His-1-carboxylate facial triad / Extradiol dioxygenase / Homoprotocatechuate 2,3-dioxygenase / Nonheme iron enzymes / Self-hydroxylationИзвор:
Journal of Biological Inorganic Chemistry, 2011, 16, 4, 589-597Издавач:
- Springer, New York
Финансирање / пројекти:
- National Institutes of Health [GM 33162, GM 072287, GM 08700]
DOI: 10.1007/s00775-011-0760-4
ISSN: 0949-8257
PubMed: 21279661
WoS: 000290284600006
Scopus: 2-s2.0-79955785664
Колекције
Институција/група
Inovacioni centar / Innovation CentreTY - JOUR AU - Farquhar, Erik R. AU - Emerson, Joseph P. AU - Koehntop, Kevin D. AU - Reynolds, Mark F. AU - Trmčić, Milena AU - Que, Jr., Lawrence PY - 2011 UR - https://cherry.chem.bg.ac.rs/handle/123456789/1335 AB - The homoprotocatechuate 2,3-dioxygenase from Arthrobacter globiformis (MndD) catalyzes the oxidative ring cleavage reaction of its catechol substrate in an extradiol fashion. Although this reactivity is more typically associated with non-heme iron enzymes, MndD exhibits an unusual specificity for manganese(II). MndD is structurally very similar to the iron(II)-dependent homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum (HPCD), and we have previously shown that both MndD and HPCD are equally active towards substrate turnover with either iron(II) or manganese(11) (Emerson et al. in Proc. Natl. Acad. Sci. USA 105:7347-7352, 2008). However, expression of MndD in Escherichia coli under aerobic conditions in the presence of excess iron results in the isolation of inactive blue-green iron-substituted MndD. Spectroscopic studies indicate that this form of iron-substituted MndD contains an iron(III) center with abound catecholate, which is presumably generated by in vivo self-hydroxylation of a second-sphere tyrosine residue, as found for other self-hydroxylated non-heme iron oxygenases. The absence of this modification in either the native manganese-containing MndD or iron-containing HPCD suggests that the metal center of iron-substituted MndD is able to bind and activate 02 in the absence of its substrate, employing a high-valence oxoiron oxidant to carry out the observed self-hydroxylation chemistry. These results demonstrate that the active site metal in MndD can support two dramatically different 02 activation pathways, further highlighting the catalytic flexibility of enzymes containing a 2-His-1-carboxylate facial triad metal binding motif. PB - Springer, New York T2 - Journal of Biological Inorganic Chemistry T1 - In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase VL - 16 IS - 4 SP - 589 EP - 597 DO - 10.1007/s00775-011-0760-4 ER -
@article{ author = "Farquhar, Erik R. and Emerson, Joseph P. and Koehntop, Kevin D. and Reynolds, Mark F. and Trmčić, Milena and Que, Jr., Lawrence", year = "2011", abstract = "The homoprotocatechuate 2,3-dioxygenase from Arthrobacter globiformis (MndD) catalyzes the oxidative ring cleavage reaction of its catechol substrate in an extradiol fashion. Although this reactivity is more typically associated with non-heme iron enzymes, MndD exhibits an unusual specificity for manganese(II). MndD is structurally very similar to the iron(II)-dependent homoprotocatechuate 2,3-dioxygenase from Brevibacterium fuscum (HPCD), and we have previously shown that both MndD and HPCD are equally active towards substrate turnover with either iron(II) or manganese(11) (Emerson et al. in Proc. Natl. Acad. Sci. USA 105:7347-7352, 2008). However, expression of MndD in Escherichia coli under aerobic conditions in the presence of excess iron results in the isolation of inactive blue-green iron-substituted MndD. Spectroscopic studies indicate that this form of iron-substituted MndD contains an iron(III) center with abound catecholate, which is presumably generated by in vivo self-hydroxylation of a second-sphere tyrosine residue, as found for other self-hydroxylated non-heme iron oxygenases. The absence of this modification in either the native manganese-containing MndD or iron-containing HPCD suggests that the metal center of iron-substituted MndD is able to bind and activate 02 in the absence of its substrate, employing a high-valence oxoiron oxidant to carry out the observed self-hydroxylation chemistry. These results demonstrate that the active site metal in MndD can support two dramatically different 02 activation pathways, further highlighting the catalytic flexibility of enzymes containing a 2-His-1-carboxylate facial triad metal binding motif.", publisher = "Springer, New York", journal = "Journal of Biological Inorganic Chemistry", title = "In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase", volume = "16", number = "4", pages = "589-597", doi = "10.1007/s00775-011-0760-4" }
Farquhar, E. R., Emerson, J. P., Koehntop, K. D., Reynolds, M. F., Trmčić, M.,& Que, Jr., L.. (2011). In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase. in Journal of Biological Inorganic Chemistry Springer, New York., 16(4), 589-597. https://doi.org/10.1007/s00775-011-0760-4
Farquhar ER, Emerson JP, Koehntop KD, Reynolds MF, Trmčić M, Que JL. In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase. in Journal of Biological Inorganic Chemistry. 2011;16(4):589-597. doi:10.1007/s00775-011-0760-4 .
Farquhar, Erik R., Emerson, Joseph P., Koehntop, Kevin D., Reynolds, Mark F., Trmčić, Milena, Que, Jr., Lawrence, "In vivo self-hydroxylation of an iron-substituted manganese-dependent extradiol cleaving catechol dioxygenase" in Journal of Biological Inorganic Chemistry, 16, no. 4 (2011):589-597, https://doi.org/10.1007/s00775-011-0760-4 . .