An effective chromatographic separation of chicken red blood cell coproporphyrinogen oxidase and uroporphyrinogen decarboxylase, two enzymes in heme biosynthesis

Jones, Marjorie A.; Taneja, M.; Xu, Yongping; Chung, Wen Jing; Stob, Christian M.; Lash, Timothy D.

doi:10.1016/j.bmcl.2004.08.065

Cited by 4 publications

(2 citation statements)

References 23 publications

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“…67 In addition, purified human recombinant CPO from Escherichia coli was isolated using the procedure reported by Medlock and Daily. 48,68 For kinetic studies, the incubation products were extracted using a microassay 69 and analyzed by HPLC.…”

Section: Action Of Cpo and Uro-d On The Diacetate Substrate 9amentioning

confidence: 99%

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Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase

Lash

Lamm

Schaber

et al. 2011

Bioorganic & Medicinal Chemistry

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Section: Action Of Cpo and Uro-d On The Diacetate Substrate 9amentioning

confidence: 99%

“…The URO-D fraction was isolated from CRH using porphyrin affinity chromatography 67. The HPLC analysis was performed on a normal phase 5 l partisil column (250 Â 4.6 mm), using a 20 lL injection loop, with a mobile phase of 35/65 v/v ethyl acetate-cyclohexane.…”

mentioning

confidence: 99%

Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase

Lash

Lamm

Schaber

et al. 2011

Bioorganic & Medicinal Chemistry

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Effects of bisphenol A on chlorophyll synthesis in soybean seedlings

Jiao

Wang

Qiu

et al. 2014

Environ Sci Pollut Res

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Bisphenol A (BPA), as an emerging environmental pollutant, is potentially harmful to plant growth. Chlorophyll (Chl) is critical in photosynthesis that provides matter and energy for plant growth. How BPA affects the chlorophyll content remains largely unknown. Here, the effects of BPA on Chl synthesis in soybean seedlings were investigated. Exposure to 1.5 mg/L BPA decreased the 5-aminolevulinic acid (ALA) content and increased protoporphyrin IX (Proto IX), magnesium protoporphyrin, and protochlorophyll contents and 5-aminolaevulinic acid dehydratase, porphobilinogen deaminase, uroporphyrinogen III synthase, uroporphyrinogen III decarboxylase, and protoporphyrinogen oxidase activities. Exposure to 17.2 and 50.0 mg/L BPA exerted the opposite effects on these four intermediates and five enzymes. Following the withdrawal of BPA exposure, the aforementioned parameters gradually recovered, except magnesium protoporphyrin content in exposure to 50.0 mg/L BPA. Our findings revealed that exposure to low-concentration BPA increased the Chl content in soybean seedlings through improving Chl synthesis, especially the conversion from ALA to Proto IX, whereas exposure to high-concentration BPA decreased the Chl content through inhibiting Chl synthesis, especially the conversion from ALA to Proto IX. The dual effects of BPA were largely reversed following the withdrawal of BPA exposure.

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The enigma of coproporphyrinogen oxidase: How does this unusual enzyme carry out oxidative decarboxylations to afford vinyl groups?

Lash

2005

Bioorganic & Medicinal Chemistry Letters

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An effective chromatographic separation of chicken red blood cell coproporphyrinogen oxidase and uroporphyrinogen decarboxylase, two enzymes in heme biosynthesis

Cited by 4 publications

References 23 publications

Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase

Normal and abnormal heme biosynthesis. Part 7. Synthesis and metabolism of coproporphyrinogen-III analogues with acetate or butyrate side chains on rings C and D. Development of a modified model for the active site of coproporphyrinogen oxidase

Effects of bisphenol A on chlorophyll synthesis in soybean seedlings

The enigma of coproporphyrinogen oxidase: How does this unusual enzyme carry out oxidative decarboxylations to afford vinyl groups?

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