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Articles

Interaction of azole antifungal antibiotics with cytochrome P -450-dependent 14α-sterol demethylase purified from Candida albicans

C A Hitchcock, K Dickinson, S B Brown, E G V Evans, D J Adams

Biochem J (1990) 266 (2): 475–480.

https://doi.org/10.1042/bj2660475

Published: 01 March 1990

View articletitled, Interaction of azole antifungal antibiotics with cytochrome P -450-dependent 14α-sterol demethylase purified from Candida albicans

Articles

Purification and properties of cytochrome P -450-dependent 14 α-sterol demethylase from Candida albicans

C A Hitchcock, K Dickinson, S B Brown, E G V Evans, D J Adams

Biochem J (1989) 263 (2): 573–579.

https://doi.org/10.1042/bj2630573

Published: 15 October 1989

View articletitled, Purification and properties of cytochrome P -450-dependent 14 α-sterol demethylase from Candida albicans

Articles

The biosynthesis of the chromophore of phycocyanin. Pathway of reduction of biliverdin to phycocyanobilin

S B Brown, J A Holroyd, D I Vernon, Y K Shim, K M Smith

Biochem J (1989) 261 (1): 259–263.

https://doi.org/10.1042/bj2610259

Published: 01 July 1989

View articletitled, The biosynthesis of the chromophore of phycocyanin. Pathway of reduction of biliverdin to phycocyanobilin

Articles

Cytochrome P -450-dependent 14 α-demethylation of lanosterol in Candida albicans

C A Hitchcock, S B Brown, E G V Evans, D J Adams

Biochem J (1989) 260 (2): 549–556.

https://doi.org/10.1042/bj2600549

Published: 01 June 1989

View articletitled, Cytochrome P -450-dependent 14 α-demethylation of lanosterol in Candida albicans

Articles

The effect of gabaculine on tetrapyrrole biosynthesis and heterotrophic growth in Cyanidium caldarium

J D Houghton, L Turner, S B Brown

Biochem J (1988) 254 (3): 907–910.

https://doi.org/10.1042/bj2540907

Published: 15 September 1988

View articletitled, The effect of gabaculine on tetrapyrrole biosynthesis and heterotrophic growth in Cyanidium caldarium

Articles

Theoretical prediction and experimental measurement of the bile-pigment isomer pattern obtained from degradation of catalase haem

N J Brindle, A C T North, S B Brown

Biochem J (1986) 236 (1): 303–306.

https://doi.org/10.1042/bj2360303

Published: 15 May 1986

View articletitled, Theoretical prediction and experimental measurement of the bile-pigment isomer pattern obtained from degradation of catalase haem

Articles

Formation of bile pigments by coupled oxidation of cobalt-substituted haemoglobin and myoglobin

D I Vernon, S B Brown

Biochem J (1984) 223 (1): 205–209.

https://doi.org/10.1042/bj2230205

Published: 01 October 1984

View articletitled, Formation of bile pigments by coupled oxidation of cobalt-substituted haemoglobin and myoglobin

Articles

Haem degradation in human haemoglobin in vitro . Separation of the contribution of the α- and β -subunits

J C Docherty, S B Brown

Biochem J (1984) 222 (2): 401–406.

https://doi.org/10.1042/bj2220401

Published: 01 September 1984

View articletitled, Haem degradation in human haemoglobin in vitro . Separation of the contribution of the α- and β -subunits

Articles

Ferrochelatase activity in the photosynthetic alga Cyanidium caldarium . Development of the enzyme during biosynthesis of photosynthetic pigments

S B Brown, J A Holroyd, D I Vernon, O T G Jones

Biochem J (1984) 220 (3): 861–863.

https://doi.org/10.1042/bj2200861

Published: 15 June 1984

View articletitled, Ferrochelatase activity in the photosynthetic alga Cyanidium caldarium . Development of the enzyme during biosynthesis of photosynthetic pigments

Articles

Biosynthesis of phycobiliproteins. Incorporation of biliverdin into phycocyanin of the red alga Cyanidium caldarium

S B Brown, J A Holroyd, D I Vernon

Biochem J (1984) 219 (3): 905–909.

https://doi.org/10.1042/bj2190905

Published: 01 May 1984

View articletitled, Biosynthesis of phycobiliproteins. Incorporation of biliverdin into phycocyanin of the red alga Cyanidium caldarium

Articles

Biosynthesis of the chromophore of phycobiliproteins. A study of mesohaem and mesobiliverdin as possible intermediates and further evidence for an algal haem oxygenase

S B Brown, J A Holroyd

Biochem J (1984) 217 (1): 265–272.

https://doi.org/10.1042/bj2170265

Published: 01 January 1984

View articletitled, Biosynthesis of the chromophore of phycobiliproteins. A study of mesohaem and mesobiliverdin as possible intermediates and further evidence for an algal haem oxygenase

Articles

A study of the mechanism of quercetin oxygenation by 18 O labelling. A comparison of the mechanism with that of haem degradation

S B Brown, V Rajananda, J A Holroyd, E G Evans

Biochem J (1982) 205 (1): 239–244.

https://doi.org/10.1042/bj2050239

Published: 01 July 1982

View articletitled, A study of the mechanism of quercetin oxygenation by 18 O labelling. A comparison of the mechanism with that of haem degradation

Articles

Bile pigment synthesis in plants. Incorporation of haem into phycocyanobilin and phycobiliproteins in Cyanidium caldarium

S B Brown, J A Holroyd, R F Troxler, G D Offner

Biochem J (1981) 194 (1): 137–147.

https://doi.org/10.1042/bj1940137

Published: 15 January 1981

View articletitled, Bile pigment synthesis in plants. Incorporation of haem into phycocyanobilin and phycobiliproteins in Cyanidium caldarium

Articles

Mechanism of bile-pigment synthesis in algae. 18 O incorporation into phycocyanobilin in the unicellular rhodophyte, Cyanidium caldarium

S B Brown, A J Holroyd, R F Troxler

Biochem J (1980) 190 (2): 445–449.

https://doi.org/10.1042/bj1900445

Published: 15 August 1980

View articletitled, Mechanism of bile-pigment synthesis in algae. 18 O incorporation into phycocyanobilin in the unicellular rhodophyte, Cyanidium caldarium

Articles

The mechanism of haem degradation in vitro . Kinetic evidence for the formation of a haem-oxygen complex

S B Brown, S E Thomas

Biochem J (1978) 176 (1): 327–330.

https://doi.org/10.1042/bj1760327

Published: 15 October 1978

View articletitled, The mechanism of haem degradation in vitro . Kinetic evidence for the formation of a haem-oxygen complex

Articles

Catalase model systems. Decomposition of hydrogen peroxide catalysed by mesoferrihaem, deuteroferrihaem, coproferrihaem and haematoferrihaem

H Hatzikonstantinou, S B Brown

Biochem J (1978) 174 (3): 893–900.

https://doi.org/10.1042/bj1740893

Published: 15 September 1978

View articletitled, Catalase model systems. Decomposition of hydrogen peroxide catalysed by mesoferrihaem, deuteroferrihaem, coproferrihaem and haematoferrihaem

Articles

The role of peroxide in haem degradation. A study of the oxidation of ferrihaems by hydrogen peroxide

S B Brown, H Hatzikonstantinou, D G Herries

Biochem J (1978) 174 (3): 901–907.

https://doi.org/10.1042/bj1740901

Published: 15 September 1978

View articletitled, The role of peroxide in haem degradation. A study of the oxidation of ferrihaems by hydrogen peroxide

Articles

Haem degradation in abnormal haemoglobins

S B Brown, J C Docherty

Biochem J (1978) 173 (3): 985–987.

https://doi.org/10.1042/bj1730985

Published: 01 September 1978

View articletitled, Haem degradation in abnormal haemoglobins

Articles

The mechanism of haem catabolism. A study of haem breakdown in spleen microsomal fraction and in a model system by 18 O labelling and metal substitution

R F G J King, S B Brown

Biochem J (1978) 174 (1): 103–109.

https://doi.org/10.1042/bj1740103

Published: 15 July 1978

View articletitled, The mechanism of haem catabolism. A study of haem breakdown in spleen microsomal fraction and in a model system by 18 O labelling and metal substitution

Articles

Phycocyanobilin synthesis in the unicellular rhodophyte Cyanidium caldarium

R F Troxler, P Kelly, S B Brown

Biochem J (1978) 172 (3): 569–576.

https://doi.org/10.1042/bj1720569

Published: 15 June 1978

View articletitled, Phycocyanobilin synthesis in the unicellular rhodophyte Cyanidium caldarium

Articles

The mechanism of haem catabolism. Bilirubin formation in living rats by [ 18 O]oxygen labelling

S B Brown, R F G J King

Biochem J (1978) 170 (2): 297–311.

https://doi.org/10.1042/bj1700297

Published: 15 February 1978

View articletitled, The mechanism of haem catabolism. Bilirubin formation in living rats by [ 18 O]oxygen labelling

Articles

Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitro

S B Brown

Biochem J (1976) 159 (1): 23–27.

https://doi.org/10.1042/bj1590023

Published: 01 October 1976

View articletitled, Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitro

Articles

Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution

S B Brown, M Shillcock, P Jones

Biochem J (1976) 153 (2): 279–285.

https://doi.org/10.1042/bj1530279

Published: 01 February 1976

View articletitled, Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution

Articles

The structure of haem in pyridine/water mixtures and its implication in studies of haem catabolism

S B Brown, R F G J King

Biochem J (1976) 153 (2): 479–483.

https://doi.org/10.1042/bj1530479

Published: 01 February 1976

View articletitled, The structure of haem in pyridine/water mixtures and its implication in studies of haem catabolism

Articles

An 18 O double-labelling study of haemoglobin catabolism in the rat

S B Brown, R F G J King

Biochem J (1975) 150 (3): 565–567.

https://doi.org/10.1042/bj1500565

Published: 01 September 1975

View articletitled, An 18 O double-labelling study of haemoglobin catabolism in the rat

Articles

Haemoglobulin catabolism: the role of ferrihaems in studies of the degradation pathway ( Short Communication )

N. A. Brown, R. F. G. J. King, M. E. Shillcock, S. B. Brown

Biochem J (1974) 137 (1): 135–137.

https://doi.org/10.1042/bj1370135

Published: 01 January 1974

View articletitled, Haemoglobulin catabolism: the role of ferrihaems in studies of the degradation pathway ( Short Communication )

Articles

Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution

S. B. Brown, T. C. Dean, Peter Jones

Biochem J (1970) 117 (4): 733–739.

https://doi.org/10.1042/bj1170733

Published: 01 May 1970

View articletitled, Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution

Articles

Catalatic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic action of ferrihaems

S. B. Brown, T. C. Dean, Peter Jones

Biochem J (1970) 117 (4): 741–744.

https://doi.org/10.1042/bj1170741

Published: 01 May 1970

View articletitled, Catalatic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic action of ferrihaems

Articles

Solution structures of ferrihaem in some dipolar aprotic solvents and their binary aqueous mixtures

S. B. Brown, I. R. Lantzke

Biochem J (1969) 115 (2): 279–285.

https://doi.org/10.1042/bj1150279

Published: 01 November 1969

View articletitled, Solution structures of ferrihaem in some dipolar aprotic solvents and their binary aqueous mixtures

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Interaction of azole antifungal antibiotics with cytochrome P -450-dependent 14α-sterol demethylase purified from Candida albicans

Purification and properties of cytochrome P -450-dependent 14 α-sterol demethylase from Candida albicans

The biosynthesis of the chromophore of phycocyanin. Pathway of reduction of biliverdin to phycocyanobilin

Cytochrome P -450-dependent 14 α-demethylation of lanosterol in Candida albicans

The effect of gabaculine on tetrapyrrole biosynthesis and heterotrophic growth in Cyanidium caldarium

Theoretical prediction and experimental measurement of the bile-pigment isomer pattern obtained from degradation of catalase haem

Formation of bile pigments by coupled oxidation of cobalt-substituted haemoglobin and myoglobin

Haem degradation in human haemoglobin in vitro . Separation of the contribution of the α- and β -subunits

Ferrochelatase activity in the photosynthetic alga Cyanidium caldarium . Development of the enzyme during biosynthesis of photosynthetic pigments

Biosynthesis of phycobiliproteins. Incorporation of biliverdin into phycocyanin of the red alga Cyanidium caldarium

Biosynthesis of the chromophore of phycobiliproteins. A study of mesohaem and mesobiliverdin as possible intermediates and further evidence for an algal haem oxygenase

A study of the mechanism of quercetin oxygenation by 18 O labelling. A comparison of the mechanism with that of haem degradation

Bile pigment synthesis in plants. Incorporation of haem into phycocyanobilin and phycobiliproteins in Cyanidium caldarium

Mechanism of bile-pigment synthesis in algae. 18 O incorporation into phycocyanobilin in the unicellular rhodophyte, Cyanidium caldarium

The mechanism of haem degradation in vitro . Kinetic evidence for the formation of a haem-oxygen complex

Catalase model systems. Decomposition of hydrogen peroxide catalysed by mesoferrihaem, deuteroferrihaem, coproferrihaem and haematoferrihaem

The role of peroxide in haem degradation. A study of the oxidation of ferrihaems by hydrogen peroxide

Haem degradation in abnormal haemoglobins

The mechanism of haem catabolism. A study of haem breakdown in spleen microsomal fraction and in a model system by 18 O labelling and metal substitution

Phycocyanobilin synthesis in the unicellular rhodophyte Cyanidium caldarium

The mechanism of haem catabolism. Bilirubin formation in living rats by [ 18 O]oxygen labelling

Stereospecific haem cleavage. A model for the formation of bile-pigment isomers in vivo and in vitro

Equilibrium and kinetic studies of the aggregation of porphyrins in aqueous solution

The structure of haem in pyridine/water mixtures and its implication in studies of haem catabolism

An 18 O double-labelling study of haemoglobin catabolism in the rat

Haemoglobulin catabolism: the role of ferrihaems in studies of the degradation pathway ( Short Communication )

Aggregation of ferrihaems. Dimerization and protolytic equilibria of protoferrihaem and deuteroferrihaem in aqueous solution

Catalatic activity of iron(III)-centred catalysts. Role of dimerization in the catalytic action of ferrihaems

Solution structures of ferrihaem in some dipolar aprotic solvents and their binary aqueous mixtures

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