TY - JOUR
T1 - Hemoglobin peroxidase reaction of hemoglobin efficiently catalyzes oxidation of benzo[a]pyrene
AU - Keum, Haein
AU - Kim, Juhee
AU - Joo, Yong Hoon
AU - Kang, Guyoung
AU - Chung, Namhyun
N1 - Funding Information:
This research was supported in part by the Hankuk University of Foreign Studies (2018). This research was also supported in part by the Institute of Life Science and Natural Resources, Korea University, Seoul, Korea (2018). This research was also supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2018R1D1A1B07049190).
Funding Information:
This research was supported in part by the Hankuk University of Foreign Studies (2018). This research was also supported in part by the Institute of Life Science and Natural Resources, Korea University, Seoul, Korea (2018). This research was also supported by Basic Science Research Program through the National Research Foundation of Korea (NRF) funded by the Ministry of Education (NRF-2018R1D1A1B07049190).
PY - 2020
Y1 - 2020
N2 - Its high molecular weight endows benzo[a]pyrene (BaP) with strong adsorption to soil, causing serious soil contamination. Our previous study has reported that hemoglobin (Hb) is able to oxidize organic pollutants in the presence of H2O2. This present study showed that Hb catalytic mechanism for BaP oxidation was similar to that of lignin peroxidase. 2-Methyl-3-vinylmaleimide was confirmed as a major degradation intermediate of BaP by Hb catalysis. In addition, BaP was shown to be degraded by heme (Hm)-catalyzed reaction, suggesting that Hm of Hb is the essential catalytic center. Rate constants (k) for BaP oxidation by Hm-catalyzed reaction were 0.4954 h−1. The major degradation intermediate by Hm-catalyzed reaction is 3,3′,5,5′-tetramethylbiphenyl. While values of Km and Vmax of Hb and Hm are very similar, kcat values was 100 times higher with Hb than with Hm. But kcat value for Hb was much lower than that for lignin peroxidase H2. All the results above suggested that Hb-catalyzed reactions efficiently degrade BaP in aqueous condition. Thus, we suggest that Hb for oxygen carrier in blood could be employed as a biocatalyst (i.e., hemoglobin peroxidase) for BaP degradation in the environment, due to the high availability of Hb.
AB - Its high molecular weight endows benzo[a]pyrene (BaP) with strong adsorption to soil, causing serious soil contamination. Our previous study has reported that hemoglobin (Hb) is able to oxidize organic pollutants in the presence of H2O2. This present study showed that Hb catalytic mechanism for BaP oxidation was similar to that of lignin peroxidase. 2-Methyl-3-vinylmaleimide was confirmed as a major degradation intermediate of BaP by Hb catalysis. In addition, BaP was shown to be degraded by heme (Hm)-catalyzed reaction, suggesting that Hm of Hb is the essential catalytic center. Rate constants (k) for BaP oxidation by Hm-catalyzed reaction were 0.4954 h−1. The major degradation intermediate by Hm-catalyzed reaction is 3,3′,5,5′-tetramethylbiphenyl. While values of Km and Vmax of Hb and Hm are very similar, kcat values was 100 times higher with Hb than with Hm. But kcat value for Hb was much lower than that for lignin peroxidase H2. All the results above suggested that Hb-catalyzed reactions efficiently degrade BaP in aqueous condition. Thus, we suggest that Hb for oxygen carrier in blood could be employed as a biocatalyst (i.e., hemoglobin peroxidase) for BaP degradation in the environment, due to the high availability of Hb.
KW - Benzo[a]pyrene
KW - Biocatalytic reaction
KW - Heme
KW - Hemoglobin
KW - Peroxidation
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U2 - 10.1016/j.chemosphere.2020.128795
DO - 10.1016/j.chemosphere.2020.128795
M3 - Article
C2 - 33143882
AN - SCOPUS:85095790624
VL - 268
JO - Chemosphere
JF - Chemosphere
SN - 0045-6535
M1 - 128795
ER -