Enzyme catalysed oxidation of ferrocene compounds

C23 Journal of Organometallic Chemistry, 134 (1977) C23-C26 0 Ebvier L&qUO~ S.A., Lae 7 Printed in The Nethedzds

Preliminary

communication

ENZY.MB CATALYSBD

OXIDATION

OF FERROCENE

COmOTJNDS

Roger Epton, Michael E. Hobson and George EIarr* Department of Physical Sciences, The Polytechnic, WV1 1LY (Great Britain) (Received

25th,

April

Wolverhampton,

1977)

Summary A facile substituted has been

transformation

ferrocenes

effected

the native

IS

known

to

give

and a series

to the corresponding

by hydrogen

or immobilized

Peroxidase,

of ferrocene

peroxide

of

ferriciniun

ions

in the presence

of

enzyme

horseradish

peroxidase.

in the presence

of hydrogen

peroxide,

to catalyse oxidation

of aromatic

the oxidation

products

depending

mines

prinarilg

and phenols

on the nature

of the substituentEl1. We report and several phthalnte

the oxidation

substituted

buffer

in the presence 0.6%

in

water)

ferrocenes,

(pH 6.1) with of horseradish

peroxide

peroxidase

in aqueous

The oxidation

solutionC2,31, and on addition

(HRP)

of

2

was allowed

concentrated

of ferricinium

correspondence

peroxide

methanol

aqueous

diamrninetetrathiocyanatochromate(II1)

* To whom

of ferrocene

in 50% methanol

hydrogen

of BBP and hydrogen

of ferrocene

a precipitate

temperature

-

(5.0 x 1GD2 m?M) (Sigma

Type

II,

as the catalyst.

The addition solution

at room

gave

to a yellow a blue

to proceed solution

(ammonium

for 4h

of ammonium

Reineckate)

diamninetetrathiocyanatochromate(II1)

should

be addressed.

u -d

P

C25

(yield

59%).(i,r:idcgticaI

The oxidation

-was deposited_ and gave (111)

that of an authentic

was repeated

hydioxymethylferriciniiun

(yield,

and hydrogen in a short

44%).

Control

peroxide

time

by hydrogen

were

experiements

necessary.to

but some oxidation

The rates

of oxidation

(equation

diamminetetrathiocyanatochromate

the absence

in

showed

effect

=%J=

-FcR + HZ02

of RRP,

did occur

of ferrocene

1; R=CH20H,

sample[4])

-with ferrocenemethanol

CHXeOH,

FcR+

that both

HRp

the oxidation

The backgrounds oxidation

(4h).

peroxide,

the 4h period

alcohols

with

of ferrocene

was negligible

after

48h

over

[5].

and the ferrocene-

CMe2OH)

were

determined

(1)

Fc = ClSHSFe (Table

1) by following

ferrocene

greater

of ferrocene convenience

of immobilized

enzyme.

acid hydrazide suspension

by hydrogen

of the immobilized was

stirred

rates

system

the bound

used

relative

We thank

at 25O,

was nonitored

and maximum

attached

via an acid

of reaction enzyme

to that

Koch-Light

azide

enzyme,

ion was effected

peroxide

gel network[6],

groups,

the supernatant

of enzyme

at 619 um for

to the ferricinium

RRP was

poly(acryloylmorpholine)

peroxide

of absorbance

and at 630 nm for the ferrocene-alcohols.

Oxidation with

the change

in tZle presence

to an activated which

contained

coupling

ferrocene

the solution

and

the initial

In the solvent

had 20% activity

of the native

A

and hydrogen

?vas centrifuged

at 619 nm to give (Table 1).

route,

per unit

weight

enzyme.

for a Research Studentship (to M!I.E.H.).

1.

A-S.

Brill

in Comprtihensive

Biological

3. Lelievre, sci.,

c. 3.

J.A. Page

5.

6.

R. Epton, in press.

Stqtz, ..

R. Gabonaud,

C.R.

Acad.-

1455. -J. Amer.

M. Rosenblum,

Chem.

(1973)

LI.Florkin and E.H.

Chem.

Sot.,

;

6146.

c. Le Feuvre 276

(1972)

and G. Wilkinson,

G. Wilkinson, J. Amer.

-~.:T :

Volume-14

Ansterd.am, 1966.

C. Le Feuvre.and

Ser C, 275

74 (1952), 4.

Elsevier,

Biochemistry,

Edited-by

Oxidations,

pp 447-449, 2.

:.;

.

References

Sot.,

E1.C. Whiting

74 (1952)

and R. Gabonaud,

and R.B; Woodward,

2125. C.R. Acad.

Sci.,

Ser C

9. M.E.

Hobson

and G. Marr,

Biochem.

Sot. Trans.,